Enzyme Nomenclature

EC 3.5.1 (continued)

In Linear Amides

Continued from EC 3.5.1.1 to EC 3.5.1.50

Contents

EC 3.5.1.51 4-acetamidobutyryl-CoA deacetylase
EC 3.5.1.52 peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
EC 3.5.1.53 N-carbamoylputrescine amidase
EC 3.5.1.54 allophanate hydrolase
EC 3.5.1.55 long-chain-fatty-acyl-glutamate deacylase
EC 3.5.1.56 N,N-dimethylformamidase
EC 3.5.1.57 tryptophanamidase
EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase
EC 3.5.1.59 N-carbamoylsarcosine amidase
EC 3.5.1.60 N-(long-chain-acyl)ethanolamine deacylase
EC 3.5.1.61 mimosinase
EC 3.5.1.62 acetylputrescine deacetylase
EC 3.5.1.63 4-acetamidobutyrate deacetylase
EC 3.5.1.64 Nα-benzyloxycarbonylleucine hydrolase
EC 3.5.1.65 theanine hydrolase
EC 3.5.1.66 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
EC 3.5.1.67 4-methyleneglutaminase
EC 3.5.1.68 N-formylglutamate deformylase
EC 3.5.1.69 glycosphingolipid deacylase
EC 3.5.1.70 aculeacin-A deacylase
EC 3.5.1.71 N-feruloylglycine deacylase
EC 3.5.1.72 D-benzoylarginine-4-nitroanilide amidase
EC 3.5.1.73 carnitinamidase
EC 3.5.1.74 chenodeoxycholoyltaurine hydrolase
EC 3.5.1.75 urethanase
EC 3.5.1.76 arylalkyl acylamidase
EC 3.5.1.77 N-carbamoyl-D-amino acid hydrolase
EC 3.5.1.78 glutathionylspermidine amidase
EC 3.5.1.79 phthalyl amidase
EC 3.5.1.80 deleted, identical to EC 3.5.1.25
EC 3.5.1.81 N-acyl-D-amino-acid deacylase
EC 3.5.1.82 N-acyl-D-glutamate deacylase
EC 3.5.1.83 N-acyl-D-aspartate deacylase
EC 3.5.1.84 biuret amidohydrolase
EC 3.5.1.85 (S)-N-acetyl-1-phenylethylamine hydrolase
EC 3.5.1.86 mandelamide amidase
EC 3.5.1.87 N-carbamoyl-L-amino-acid hydrolase
EC 3.5.1.88 peptide deformylase
EC 3.5.1.89 N-acetylglucosaminylphosphatidylinositol deacetylase
EC 3.5.1.90 adenosylcobinamide hydrolase
EC 3.5.1.91 N-substituted formamide deformylase
EC 3.5.1.92 pantetheine hydrolase
EC 3.5.1.93 glutaryl-7-aminocephalosporanic-acid acylase
EC 3.5.1.94 γ-glutamyl-γ-aminobutyrate hydrolase
EC 3.5.1.95 N-malonylurea hydrolase
EC 3.5.1.96 succinylglutamate desuccinylase
EC 3.5.1.97 acyl-homoserine-lactone acylase
EC 3.5.1.98 histone deacetylase
EC 3.5.1.99 fatty acid amide hydrolase
EC 3.5.1.100 (R)-amidase
EC 3.5.1.101 L-proline amide hydrolase
EC 3.5.1.102 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
EC 3.5.1.103 N-acetyl-1D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase
EC 3.5.1.104 peptidoglycan-N-acetylglucosamine deacetylase
EC 3.5.1.105 chitin disaccharide deacetylase
EC 3.5.1.106 N-formylmaleamate deformylase
EC 3.5.1.107 maleamate amidohydrolase
EC 3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine deacetylase
EC 3.5.1.109 sphingomyelin deacylase
EC 3.5.1.110 peroxyureidoacrylate/ureidoacrylate amidohydrolase
EC 3.5.1.111 2-oxoglutaramate amidase
EC 3.5.1.112 2'-N-acetylparomamine deacetylase
EC 3.5.1.113 2'''-acetyl-6'''-hydroxyneomycin C deacetylase
EC 3.5.1.114 N-acyl-aromatic-L-amino acid amidohydrolase
EC 3.5.1.115 mycothiol S-conjugate amidase
EC 3.5.1.116 ureidoglycolate amidohydrolase
EC 3.5.1.117 6-aminohexanoate-oligomer endohydrolase
EC 3.5.1.118 γ-glutamyl hercynylcysteine S-oxide hydrolase
EC 3.5.1.119 Pup deamidase
EC 3.5.1.120 transferred, now EC 3.5.99.11
EC 3.5.1.121 protein N-terminal asparagine amidohydrolase
EC 3.5.1.122 protein N-terminal glutamine amidohydrolase
EC 3.5.1.123 γ-glutamylanilide hydrolase
EC 3.5.1.124 protein deglycase
EC 3.5.1.125 N2-acetyl-L-2,4-diaminobutanoate deacetylase
EC 3.5.1.126 oxamate amidohydrolase
EC 3.5.1.127 jasmonoyl-L-amino acid hydrolase
EC 3.5.1.128 deaminated glutathione amidase
EC 3.5.1.129 N5-(cytidine 5′-diphosphoramidyl)-L-glutamine hydrolase
EC 3.5.1.130 [lysine-biosynthesis-protein LysW]-lysine/ornithine hydrolase
EC 3.5.1.131 1-carboxybiuret hydrolase
EC 3.5.1.132 [amino group carrier protein]-ornithine hydrolase

Entries

EC 3.5.1.51

Accepted name: 4-acetamidobutyryl-CoA deacetylase

Reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA

Other name(s): aminobutyryl-CoA thiolesterase; deacetylase-thiolesterase

Systematic name: 4-acetamidobutanoyl-CoA amidohydrolase

Comments: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ohsugi, M., Khan, J., Hensley, C., Chew, S. and Barker, H.A. Metabolism of L-β-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. J. Biol. Chem. 256 (1981) 7642-7651. [PMID: 6788773]

[EC 3.5.1.51 created 1984]

EC 3.5.1.52

Accepted name: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase

Reaction: Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue

Other name(s): glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase

Systematic name: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase

Comments: Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 83534-39-8

References:

1. Plummer, T.H., Jr. and Tarentino, A.L. Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase. J. Biol. Chem. 256 (1981) 10243-10246. [PMID: 7287707]

2. Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194-1201. [PMID: 901470]

3. Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467-1473. [PMID: 738997]

4. Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24 (1985) 4665-4671. [PMID: 4063349]

[EC 3.5.1.52 created 1984, modified 1989 (EC 3.2.2.18 created 1984, incorporated 1989)]

EC 3.5.1.53

Accepted name: N-carbamoylputrescine amidase

Reaction: N-carbamoylputrescine + H2O = putrescine + CO2 + NH3

Other name(s): carbamoylputrescine hydrolase; NCP

Systematic name: N-Carbamoylputrescine amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 85030-69-9

References:

1. Yanagisawa, H. and Suzuki, Y. Preparation and properties of N-carbamylputrescine amidohydrolase from maize shoots. Phytochemistry 21 (1982) 2201-2203.

[EC 3.5.1.53 created 1986]

EC 3.5.1.54

Accepted name: allophanate hydrolase

Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3

For diagram of reaction click here.

Glossary: allophanate = urea-1-carboxylate

Other name(s): allophanate lyase; AtzF; TrzF

Systematic name: urea-1-carboxylate amidohydrolase

Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 79121-96-3

References:

1. Maitz, G.S., Haas, E.M. and Castric, P.A. Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii. Biochim. Biophys. Acta 714 (1982) 486-491.

2. Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107-4113. [PMID: 4556303]

3. Sumrada, R.A. and Cooper, T.G. Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. J. Biol. Chem. 257 (1982) 9119-9127. [PMID: 6124544]

4. Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. FEMS Microbiol. Lett. 245 (2005) 61-65. [PMID: 15796980]

5. Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437-4445. [PMID: 16085834]

6. Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731-3738. [PMID: 15901697]

7. Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491-2495. [PMID: 16597948]

[EC 3.5.1.54 created 1986, modified 2008]

EC 3.5.1.55

Accepted name: long-chain-fatty-acyl-glutamate deacylase

Reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate

Other name(s): long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase

Systematic name: N-long-chain-fatty-acyl-L-glutamate amidohydrolase

Comments: Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82249-69-2

References:

1. Fukuda, H., Iwade, S. and Kimura, A. A new enzyme: long acyl aminoacylase from Pseudomonas diminuta. J. Biochem. (Tokyo) 91 (1982) 1731-1738. [PMID: 7096313]

[EC 3.5.1.55 created 1986]

EC 3.5.1.56

Accepted name: N,N-dimethylformamidase

Reaction: N,N-dimethylformamide + H2O = dimethylamine + formate

Other name(s): dimethylformamidase; DMFase

Systematic name: N,N-dimethylformamide amidohydrolase

Comments: An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-73-0

References:

1. Schär, H.-P., Holzmann, W., Ramos Tombo, G.M. and Ghisalba, O. Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3. Eur. J. Biochem. 158 (1986) 469-475. [PMID: 3732281]

[EC 3.5.1.56 created 1989]

EC 3.5.1.57

Accepted name: tryptophanamidase

Reaction: L-tryptophanamide + H2O = L-tryptophan + NH3

Other name(s): tryptophan aminopeptidase; L-tryptophan aminopeptidase

Systematic name: L-tryptophanamide amidohydrolase

Comments: Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 76689-19-5

References:

1. Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M. Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum. Agric. Biol. Chem. 47 (1983) 2483-2493.

[EC 3.5.1.57 created 1989]

EC 3.5.1.58

Accepted name: N-benzyloxycarbonylglycine hydrolase

Reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine

Other name(s): benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I

Systematic name: N-benzyloxycarbonylglycine urethanehydrolase

Comments: Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64 Nα-benzyloxycarbonylleucine hydrolase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 91930-69-7

References:

1. Murao, S., Matsumura, E. and Kawano, T. Isolation and characterization of a novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043. Agric. Biol. Chem. 49 (1985) 967-972.

[EC 3.5.1.58 created 1989]

EC 3.5.1.59

Accepted name: N-carbamoylsarcosine amidase

Reaction: N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3

For diagram of reaction click here.

Other name(s): carbamoylsarcosine amidase

Systematic name: N-carbamoylsarcosine amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 92767-52-7

References:

1. Deeg, R., Roeder, A., Siedel, J., Gauhl, H. and Ziegenhorn, J. Process and reagent for the determination of N-carbamoylsarcosine with the use of a new enzyme. Patent DE3248145, 1982, Chem. Abstr. 101 (1984) 187515.

[EC 3.5.1.59 created 1989]

EC 3.5.1.60

Accepted name: N-(long-chain-acyl)ethanolamine deacylase

Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine

Other name(s): N-acylethanolamine amidohydrolase; acylethanolamine amidase

Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase

Comments: Does not act on N-acylsphingosine or N,O-diacylethanolamine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99283-61-1

References:

1. Schmid, P.C., Zuzarte-Augustin, M.L. and Schmid, H.H.O. Properties of rat liver N-acylethanolamine amidohydrolase. J. Biol. Chem. 260 (1985) 14145-14149. [PMID: 4055775]

[EC 3.5.1.60 created 1989]

EC 3.5.1.61

Accepted name: mimosinase

Reaction: (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O = 3-hydroxy-4H-pyrid-4-one + L-serine

Systematic name: mimosine amidohydrolase

Comments: An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104118-49-2

References:

1. Tangendjaja, B., Lowry, J.B. and Wills, R.H. Isolation of a mimosine degrading enzyme from Leucaena leaf. J. Sci. Food Agric. 37 (1986) 523-526.

[EC 3.5.1.61 created 1989]

EC 3.5.1.62

Accepted name: acetylputrescine deacetylase

Reaction: N-acetylputrescine + H2O = acetate + putrescine

Glossary: spermidine

Systematic name: N-acetylputrescine acetylhydrolase

Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 103679-48-7

References:

1. Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140-142.

[EC 3.5.1.62 created 1989]

EC 3.5.1.63

Accepted name: 4-acetamidobutyrate deacetylase

Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate

Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA

Systematic name: 4-acetamidobutanoate amidohydrolase

Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102347-82-0

References:

1. Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7-14.

[EC 3.5.1.63 created 1989]

EC 3.5.1.64

Accepted name: Nα-benzyloxycarbonylleucine hydrolase

Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine

Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV

Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase

Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100630-47-5

References:

1. Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643-3645.

[EC 3.5.1.64 created 1989]

EC 3.5.1.65

Accepted name: theanine hydrolase

Reaction: N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine

Glossary: L-theanine = N5-ethyl-L-glutamine

Systematic name: N5-ethyl-L-glutamine amidohydrolase

Comments: Also acts on other N-alkyl-L-glutamines.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99533-51-4

References:

1. Tsushida, T. and Takeo, T. An enzyme hydrolyzing L-theanine in tea leaves. Agric. Biol. Chem. 49 (1985) 2913-2917.

[EC 3.5.1.65 created 1989]

EC 3.5.1.66

Accepted name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase

Reaction: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2

Other name(s): compound B hydrolase; α-hydroxymethyl-α'-(N-acetylaminomethylene)succinic acid hydrolase

Systematic name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)

Comments: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 95829-26-8

References:

1. Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379-2383. [PMID: 3972793]

[EC 3.5.1.66 created 1989]

EC 3.5.1.67

Accepted name: 4-methyleneglutaminase

Reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3

Other name(s): 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase

Systematic name: 4-methylene-L-glutamine amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 86855-36-9

References:

1. Ibrahim, S.A., Lea, P.J. and Fowden, L. Preparation and properties of 4-methyleneglutaminase from the leaves of peanut (Arachis hypogaea). Phytochemistry 23 (1984) 1545-1549.

[EC 3.5.1.67 created 1989]

EC 3.5.1.68

Accepted name: N-formylglutamate deformylase

Reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate

For diagram click here.

Other name(s): β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citrylglutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme

Systematic name: N-formyl-L-glutamate amidohydrolase

Comments: The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97286-12-9

References:

1. Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696-4702. [PMID: 3308850]

2. Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206-214. [PMID: 6414521]

[EC 3.5.1.68 created 1989]

EC 3.5.1.69

Accepted name: glycosphingolipid deacylase

Reaction: Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives

Other name(s): glycosphingolipid ceramide deacylase

Systematic name: glycosphingolipid amidohydrolase

Comments: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122544-53-0

References:

1. Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1-4. [PMID: 3360750]

[EC 3.5.1.69 created 1990]

EC 3.5.1.70

Accepted name: aculeacin-A deacylase

Reaction: Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain

Other name(s): aculeacin A acylase

Systematic name: aculeacin-A amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-50-3

References:

1. Takeshima, H., Inokoshi, J., Takada, Y., Tanaka, H. and Omura, S. A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J. Biochem. (Tokyo) 105 (1989) 606-610. [PMID: 2760018]

[EC 3.5.1.70 created 1992]

EC 3.5.1.71

Accepted name: N-feruloylglycine deacylase

Reaction: N-feruloylglycine + H2O = ferulate + glycine

Other name(s): N-feruloylglycine hydrolase

Systematic name: N-feruloylglycine amidohydrolase

Comments: Hydrolyses a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118731-84-3

References:

1. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. N-Feruloylglycine amidohydrolase from barley seeds and isolated barley embryos. Phytochemistry 27 (1988) 2457-2463.

2. Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., CASteele, K.V. and Van Sumere, F. Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos. Phytochemistry 27 (1988) 2465-2475.

[EC 3.5.1.71 created 1992]

EC 3.5.1.72

Accepted name: D-benzoylarginine-4-nitroanilide amidase

Reaction: N-benzoyl-D-arginine-4-nitroanilide + H2O = N-benzoyl-D-arginine + 4-nitroaniline

Other name(s): benzoyl-D-arginine arylamidase; D-BAPA-ase

Systematic name: N-benzoyl-D-arginine-4-nitroanilide amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119345-26-5

References:

1. Gofshtein-Gandman, L.V., Keynan, A. and Milner, Y. Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide. J. Bacteriol. 170 (1988) 5895-5900. [PMID: 3142860]

[EC 3.5.1.72 created 1992]

EC 3.5.1.73

Accepted name: carnitinamidase

Reaction: L-carnitinamide + H2O = L-carnitine + NH3

Other name(s): L-carnitinamidase; carnitine amidase; L-carnitine amidase

Systematic name: L-carnitinamide amidohydrolase

Comments: Does not act on D-carnitinamide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 117444-04-9

References:

1. Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for producing carnitine, L-carnitinamide hydrolase and method for producing same. Patent DE3728321, 1988, Chem. Abstr. 109 (1988) 228738.

[EC 3.5.1.73 created 1992]

EC 3.5.1.74

Accepted name: chenodeoxycholoyltaurine hydrolase

Reaction: chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine

Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate

Systematic name: chenodeoxycholoyltaurine amidohydrolase

Comments: Some other taurine conjugates are hydrolysed, but not glycine conjugates of bile acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125752-75-2

References:

1. Kawamoto, K., Horibe, I. and Uchida, K. Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. (Tokyo) 106 (1989) 1049-1053. [PMID: 2628421]

[EC 3.5.1.74 created 1992]

EC 3.5.1.75

Accepted name: urethanase

Reaction: urethane + H2O = ethanol + CO2 + NH3

Other name(s): urethane hydrolase

Systematic name: urethane amidohydrolase (decarboxylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122007-70-9

References:

1. Kobashi, K., Takebe, S. and Sakai, T. Urethane-hydrolyzing enzyme from Citrobacter sp. Chem. Pharm. Bull. 38 (1990) 1326-1328. [PMID: 2393957]

[EC 3.5.1.75 created 1992]

EC 3.5.1.76

Accepted name: arylalkyl acylamidase

Reaction: N-acetylarylalkylamine + H2O = arylalkylamine + acetate

Other name(s): aralkyl acylamidase

Systematic name: N-acetylarylalkylamine amidohydrolase

Comments: identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Shimizu, S., Ogawa, J., Chung, M.C.-M., Yamada, H. Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2. Eur. J. Biochem. 209 (1992) 375-382. [PMID: 1396711]

[EC 3.5.1.76 created 1999]

EC 3.5.1.77

Accepted name: N-carbamoyl-D-amino-acid hydrolase

Reaction: an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2

Other name(s): D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase

Systematic name: N-carbamoyl-D-amino-acid amidohydrolase

Comments: This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71768-08-6

References:

1. Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685-691. [PMID: 8462543]

2. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]

[EC 3.5.1.77 created 1999, modified 2008]

EC 3.5.1.78

Accepted name: glutathionylspermidine amidase

Reaction: glutathionylspermidine + H2O = glutathione + spermidine

For diagram of reaction click here.

Glossary: spermidine

Other name(s): glutathionylspermidine amidohydrolase (spermidine-forming)

Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase

Comments: spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 171040-71-4

References:

1. Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031-14041. [PMID: 7775463]

[EC 3.5.1.78 created 1999]

EC 3.5.1.79

Accepted name: phthalyl amidase

Reaction: a phthalylamide + H2O = phthalic acid + a substituted amine

Systematic name: phthalyl-amide amidohydrolase

Comments: in the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, β-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 169150-79-2

References:

1. Briggs, B.S., Kreuzman, A.J., Whitesitt, C., Yeh, W.K., Zmijewski, M. Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis. J. Mol. Catal., B Enzym. 2 (1996) 53-69.

2. Black, T.D., Briggs, B.S., Evans, R., Muth, W.L., Vangala, S., Zmijewski, M.J. o-Phthalyl amidase in the synthesis of Loracarbef: process development using this novel biocatalyst. Biotechnol. Lett. 18 (1996) 875-880.

3. Costello, C., Kreuzman, A., Zmijewski, M. Selective deprotection of phthalyl protected proteins. Tetrahedron Lett. 37 (1996) 7469-7472.

4. Briggs, B.S., Zmijewski, M.J. Enzyme from microbial source: phthalyl amidase. Patent US5445959, 1995. Chem. Abstr. 123 (1995) 250104 (PDF).

[EC 3.5.1.79 created 1999]

[EC 3.5.1.80 Deleted entry: identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.80 created 1999, deleted 2002)]

EC 3.5.1.81

Accepted name: N-acyl-D-amino-acid deacylase

Reaction: N-acyl-D-amino acid + H2O = a carboxylate + D-amino acid

Systematic name: N-acyl-D-amino acid amidohydrolase

Comments: The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65979-42-2

References:

1. Wakayama, M., Katsuno, Y., Hayashi, S., Miyamoto, Y., Sakai, K. and Moriguchi, M. Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli. Biosci. Biotechnol. Biochem. 59 (1995) 2115-2119. [PMID: 8541651]

2. Wakayama, M., Hayashi, S., Yatsuda, Y., Katsuno, Y., Sakai, K. and Moriguchi, M. Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification. Protein Expr. Purif. 7 (1996) 395-399. [PMID: 8776758]

[EC 3.5.1.81 created 1999]

EC 3.5.1.82

Accepted name: N-acyl-D-glutamate deacylase

Reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate

Systematic name: N-acyl-D-glutamate amidohydrolase

Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82249-69-2

References:

1. Wakayama, M., Ahshika, T., Miyamoto, Y., Yoshikawa, T., Sonoda, Y., Sakai, K. and Moriguchi, M. Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Biochem. (Tokyo) 118 (1995) 204-209. [PMID: 8537313]

2. Wakayama, M., Miura, Y., Oshima, K., Sakai, K. and Moriguchi, M. Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1. Biosci. Biotechnol. Biochem. 59 (1995) 1489-1492. [PMID: 7549100]

3. Wakayama, M., Tsutsumi, T., Yada, H., Sakai, K. and Moriguchi, M. Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1. Biosci. Biotechnol. Biochem. 60 (1996) 650-653. [PMID: 8829533]

[EC 3.5.1.82 created 1999]

EC 3.5.1.83

Accepted name: N-acyl-D-aspartate deacylase

Reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate

Systematic name: N-acyl-D-aspartate amidohydrolase

Comments: the enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-86-1

References:

1. Moriguchi, M., Sakai, K., Katsuno, Y., Maki, T., Wakayama, M. Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. Biosci. Biotechnol. Biochem. 57 (1993) 1145-1148. [PMID: 7763985]

2. Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y., Sakai, K., Moriguchi, M. Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Ferment. Bioeng. 80 (1995) 311-317.

[EC 3.5.1.83 created 1999]

EC 3.5.1.84

Accepted name: biuret amidohydrolase

Reaction: biuret + H2O = urea-1-carboxylate + NH3

For diagram of reaction click here.

Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate

Other name(s): biuH (gene name)

Systematic name: biuret amidohydrolase

Comments: The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, UM-BBD, CAS registry number: 95567-88-7

References:

1. Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s-triazine ring metabolism. ACS Catal. 2011 (2011) 1075-1082. [PMID: 21897878]

2. Esquirol, L., Peat, T.S., Wilding, M., Lucent, D., French, N.G., Hartley, C.J., Newman, J. and Scott, C. Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminosarum bv. viciae 3841. PLoS One 13 (2018) e0192736. [PMID: 29425231]

3. Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem 293 (2018) 7880-7891. [PMID: 29523689]

[EC 3.5.1.84 created 2000, modified 2008, modified 2019]

EC 3.5.1.85

Accepted name: (S)-N-acetyl-1-phenylethylamine hydrolase

Reaction: N-acetylphenylethylamine + H2O = phenylethylamine + acetate

Other name: (S)-N-acetyl-1-phenylethylamine amidohydrolase

Systematic name: (S)-N-acetylphenylethylamine:H2O hydrolase

Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 192230-94-7

References:

1. Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515-520.

[EC 3.5.1.85 created 2000, modified 2002]

EC 3.5.1.86

Accepted name: mandelamide amidase

Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3

Glossary: (R)-mandelate = (R)-2-hydroxy-2-phenylacetate

Other name(s): Pseudomonas mandelamide hydrolase

Systematic name: mandelamide hydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(–)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028-3032. [PMID: 1660699]

[EC 3.5.1.86 created 2000]

EC 3.5.1.87

Accepted name: N-carbamoyl-L-amino-acid hydrolase

Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2

Other name(s): N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous)

Systematic name: N-carbamoyl-L-amino-acid amidohydrolase

Comments: This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Ogawa, J., Miyake, H. and Shimizu, S. Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol. 43 (1995) 1039-1043. [PMID: 8590654]

2. Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9 (2005) 16-25. [PMID: 16254442]

3. Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559-563. [PMID: 11849938]

[EC 3.5.1.87 created 2001, modified 2008]

EC 3.5.1.88

Accepted name: peptide deformylase

Reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide

Systematic name: formyl-L-methionyl peptide amidohydrolase

Comments: Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.27 (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31 (formylmethionine deformylase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 369636-51-1

References:

1. Adams, J.M. On the release of the formyl group from nascent protein. J. Mol. Biol. 33 (1968) 571-589. [PMID: 4973445]

2. Mazel, D., Pochet, S. and Marliere, P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13 (1994) 914-923. [PMID: 8112305]

3. Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D. Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36 (1997) 13904-13909. [PMID: 9374869]

4. Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273 (1998) 11413-11416. [PMID: 9565550]

5. Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F. Iron center, substrate recognition, and mechanism of peptide deformylase. Nat. Struct. Biol. 5 (1998) 1053-1058. [PMID: 9846875]

6. Rajagopalan, P.T.R., Yu, X.C. and Pei, D. Peptide deformylase: a new type of mononuclear iron protein. J. Am. Chem. Soc. 119 (1997) 12418-12419.

7. Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246 (1998) 342-346. [PMID: 9610360]

8. Rajagopalan, P.T.R., Grimme, S. and Pei, D. Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39 (2000) 779-790. [PMID: 10651644]

9. Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D. Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38 (1999) 643-650. [PMID: 9888804]

10. Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J. Mol. Biol. 289 (1999) 1445-1457. [PMID: 10373378]

11. Giglione, C., Pierre, M. and Meinnel, T. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36 (2000) 1197-1205. [PMID: 10931273]

12. Pei, D. Peptide deformylase: a target for novel antibiotics? Emerging Therapeutic Targets 5 (2001) 23-40.

[EC 3.5.1.88 created 2001]

EC 3.5.1.89

Accepted name: N-acetylglucosaminylphosphatidylinositol deacetylase

Reaction: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate

For diagram click here.

Other name(s): N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase

Systematic name: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase

Comments: Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122191-30-4

References:

1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]

2. Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834-15840. [PMID: 9188481]

3. Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185-192. [PMID: 10085243]

4. Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322-3332. [PMID: 11432820]

[EC 3.5.1.89 created 1992 as EC 3.1.1.69, transferred 2002 to EC 3.5.1.89, modified 2002]

EC 3.5.1.90

Accepted name: adenosylcobinamide hydrolase

Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol

For diagram click here.

Other name(s): CbiZ; AdoCbi amidohydrolase

Systematic name: adenosylcobinamide amidohydrolase

Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 905988-16-1

References:

1. Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591-3596. [PMID: 14990804]

[EC 3.5.1.90 created 2004]

EC 3.5.1.91

Accepted name: N-substituted formamide deformylase

Reaction: N-benzylformamide + H2O = formate + benzylamine

For diagram click here.

Other name(s): NfdA

Systematic name: N-benzylformamide amidohydrolase

Comments: Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 115299-95-1

References:

1. Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H. and Kobayashi, M. Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning. Proc. Natl. Acad. Sci. USA 101 (2004) 13726-13731. [PMID: 15358859]

[EC 3.5.1.91 created 2005]

EC 3.5.1.92

Accepted name: pantetheine hydrolase

Reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol

Other name(s): pantetheinase; vanin; vanin-1

Systematic name: (R)-pantetheine amidohydrolase

Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol, a potent anti-oxidant [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56093-18-6

References:

1. Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262-267. [PMID: 440106]

2. Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175-181. [PMID: 6549111]

3. Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149-152. [PMID: 10567687]

4. Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391-405. [PMID: 8934567]

5. Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Dupre, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149-154. [PMID: 11042271]

6. Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296-306. [PMID: 11491533]

7. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-001.9. [PMID: 11380987]

[EC 3.5.1.92 created 2005]

EC 3.5.1.93

Accepted name: glutaryl-7-aminocephalosporanic-acid acylase

Reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate

For diagram click here.

Other name(s): 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase

Systematic name: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase

Comments: Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56645-46-6

References:

1. Ishii, Y., Saito, Y., Fujimura, T., Sasaki, H., Noguchi, Y., Yamada, H., Niwa, M. and Shimomura, K. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230 (1995) 773-778. [PMID: 7607251]

2. Kinoshita, T., Tada, T., Saito, Y., Ishii, Y., Sato, A. and Murata, M. Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 458-459. [PMID: 10739919]

3. Monti, D., Carrea, G., Riva, S., Baldaro, E. and Frare, G. Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Biotechnol. Bioeng. 70 (2000) 239-244. [PMID: 10972935]

4. Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S. and Kim, K.H. Crystallization and preliminary X-ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. J. Struct. Biol. 131 (2000) 79-81. [PMID: 10945972]

5. Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. and Hol, W.G.J. The 2.0 Å crystal structure of cephalosporin acylase. Structure Fold Des. 8 (2000) 1059-1068. [PMID: 11080627]

6. Huang, X., Zeng, R., Ding, X., Mao, X., Ding, Y., Rao, Z., Xie, Y., Jiang, W. and Zhao, G. Affinity alkylation of the Trp-B4 residue of the β-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277 (2002) 10256-10264. [PMID: 11782466]

7. Kim, J.K., Yang, I.S., Rhee, S., Dauter, Z., Lee, Y.S., Park, S.S. and Kim, K.H. Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42 (2003) 4084-4093. [PMID: 12680762]

[EC 3.5.1.93 created 2005]

EC 3.5.1.94

Accepted name: γ-glutamyl-γ-aminobutyrate hydrolase

Reaction: 4-(γ-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate

Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA

Other name(s): γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase

Systematic name: 4-(γ-L-glutamylamino)butanoate amidohydrolase

Comments: Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602-4608. [PMID: 15590624]

[EC 3.5.1.94 created 2006, modified 2011]

EC 3.5.1.95

Accepted name: N-malonylurea hydrolase

Reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea

For diagram, click here

Other name(s): ureidomalonase

Systematic name: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)

Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 368888-22-6

References:

1. Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222-226. [PMID: 11485332]

2. Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051-7058. [PMID: 11748240]

[EC 3.5.1.95 created 2006]

EC 3.5.1.96

Accepted name: succinylglutamate desuccinylase

Reaction: N-succinyl-L-glutamate + H2O = succinate + L-glutamate

For diagram, click here

Other name(s): N2-succinylglutamate desuccinylase; SGDS; AstE

Systematic name: N-succinyl-L-glutamate amidohydrolase

Comments: Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 99676-40-1

References:

1. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]

2. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]

3. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]

4. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]

[EC 3.5.1.96 created 2006]

EC 3.5.1.97

Accepted name: acyl-homoserine-lactone acylase

Reaction: an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate

Other name(s): acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; PvdQ; QuiP

Systematic name: N-acyl-L-homoserine-lactone amidohydrolase

Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3′-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Sio, C.F., Otten, L.G., Cool, R.H., Diggle, S.P., Braun, P.G., Bos, R., Daykin, M., Cámara, M., Williams, P. and Quax, W.J. Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1. Infect. Immun. 74 (2006) 1673-1682. [PMID: 16495538]

2. Lin, Y.H., Xu, J.L., Hu, J., Wang, L.H., Ong, S.L., Leadbetter, J.R. and Zhang, L.H. Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol. 47 (2003) 849-860. [PMID: 12535081]

[EC 3.5.1.97 created 2007]

EC 3.5.1.98

Accepted name: histone deacetylase

Reaction: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone

Other name(s): HDAC

Systematic name: histone amidohydrolase

Comments: A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Krieger, D.E., Levine, R., Merrifield, R.B., Vidali, G. and Allfrey, V.G. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei. J. Biol. Chem. 249 (1974) 332-334. [PMID: 4855628]

2. Sanchez del Pino, M.M., Lopez-Rodas, G., Sendra, R. and Tordera, V. Properties of the yeast nuclear histone deacetylase. Biochem. J. 303 (1994) 723-729. [PMID: 7980438]

3. Ouaissi, M. and Ouaissi, A. Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases. J. Biomed. Biotechnol. 2006 (2006) 13474 only. [PMID: 16883049]

4. Song, Y.M., Kim, Y.S., Kim, D., Lee, D.S. and Kwon, H.J. Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24. Biochem. Biophys. Res. Commun. 361 (2007) 55-61. [PMID: 17632079]

5. Finnin, M.S., Donigian, J.R., Cohen, A., Richon, V.M., Rifkind, R.A., Marks, P.A., Breslow, R. and Pavletich, N.P. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193. [PMID: 10490031]

6. Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A. and Klein, P.S. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276 (2001) 36734-36741. [PMID: 11473107]

7. de Ruijter, A.J., van Gennip, A.H., Caron, H.N., Kemp, S. and van Kuilenburg, A.B. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. 370 (2003) 737-749. [PMID: 12429021]

[EC 3.5.1.98 created 2008]

EC 3.5.1.99

Accepted name: fatty acid amide hydrolase

Reaction: (1) anandamide + H2O = arachidonic acid + ethanolamine
(2) oleamide + H2O = oleic acid + NH3

Glossary: anandamide = (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide

Other name(s): FAAH; oleamide hydrolase; anandamide amidohydrolase

Systematic name: fatty acylamide amidohydrolase

Comments: Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Boger, D.L., Fecik, R.A., Patterson, J.E., Miyauchi, H., Patricelli, M.P. and Cravatt, B.F. Fatty acid amide hydrolase substrate specificity. Bioorg. Med. Chem. Lett. 10 (2000) 2613-2616. [PMID: 11128635]

2. Patricelli, M.P., Lashuel, H.A., Giang, D.K., Kelly, J.W. and Cravatt, B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry 37 (1998) 15177-15187. [PMID: 9790682]

3. Patricelli, M.P. and Cravatt, B.F. Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40 (2001) 6107-6115. [PMID: 11352748]

[EC 3.5.1.99 created 2009]

EC 3.5.1.100

Accepted name: (R)-amidase

Reaction: (1) (R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + NH3
(2) β-alaninamide + H2O = β-alanine + NH3

Other name(s): R-stereospecific amidase; R-amidase

Systematic name: (R)-piperazine-2-carboxamide amidohydrolase

Comments: In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide. Eur. J. Biochem. 271 (2004) 1580-1590. [PMID: 15066183]

[EC 3.5.1.100 created 2009, modified 2011]

EC 3.5.1.101

Accepted name: L-proline amide hydrolase

Reaction: (1) (S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3
(2) L-prolinamide + H2O = L-proline + NH3

Glossary: L-pipecolate = piperidine-2-carboxylate

Other name(s): S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase

Systematic name: (S)-piperidine-2-carboxamide amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase. Eur. J. Biochem. 271 (2004) 1465-1475. [PMID: 15066172]

[EC 3.5.1.101 created 2009]

EC 3.5.1.102

Accepted name: 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase

Reaction: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate

Other name(s): ArfB

Systematic name: 2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase

Comments: The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181-4188. [PMID: 19309161]

[EC 3.5.1.102 created 2010, modified 2011]

EC 3.5.1.103

Accepted name: N-acetyl-1D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase

Reaction: 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + acetate

For diagram of reaction click here

Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol

Other name(s): MshB

Systematic name: 1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase

Comments: This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341-1349. [PMID: 12724395]

2. Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958-6963. [PMID: 11092856]

3. Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166-47170. [PMID: 12958317]

[EC 3.5.1.103 created 2010]

EC 3.5.1.104

Accepted name: peptidoglycan-N-acetylglucosamine deacetylase

Reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate

Other name(s): HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase

Systematic name: peptidoglycan-N-acetylglucosamine amidohydrolase

Comments: Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and Bouriotis, V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J. Biol. Chem. 280 (2005) 30856-30863. [PMID: 15961396]

2. Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and Kokkinidis, M. Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 203-205. [PMID: 18323609]

3. Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and van Aalten, D.M. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. USA 102 (2005) 15429-15434. [PMID: 16221761]

4. Wang, G., Olczak, A., Forsberg, L.S. and Maier, R.J. Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J. Biol. Chem. 284 (2009) 6790-6800. [PMID: 19147492]

5. Popowska, M., Kusio, M., Szymanska, P. and Markiewicz, Z. Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J Microbiol Biotechnol 19 (2009) 932-945. [PMID: 19809250]

6. Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and Gottschalk, M. Significant contribution of the pgdA gene to the virulence of Streptococcus suis. Mol. Microbiol. 70 (2008) 1120-1135. [PMID: 18990186]

[EC 3.5.1.104 created 2010]

EC 3.5.1.105

Accepted name: chitin disaccharide deacetylase

Reaction: N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate

Other name(s): chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase

Systematic name: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase

Comments: Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahaemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357-365. [PMID: 17334758]

2. Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046-1053. [PMID: 19553519]

3. Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113-1117.

4. Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561-563. [PMID: 16232910]

[EC 3.5.1.105 created 2010]

EC 3.5.1.106

Accepted name: N-formylmaleamate deformylase

Reaction: N-formylmaleamic acid + H2O = maleamate + formate

Other name(s): NicD

Systematic name: N-formylmaleamic acid amidohydrolase

Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]

[EC 3.5.1.106 created 2010]

EC 3.5.1.107

Accepted name: maleamate amidohydrolase

Reaction: maleamate + H2O = maleate + NH3

Other name(s): NicF

Systematic name: maleamate amidohydrolase

Comments: The reaction is involved in the aerobic catabolism of nicotinic acid.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]

[EC 3.5.1.107 created 2010]

EC 3.5.1.108

Accepted name: UDP-3-O-acyl-N-acetylglucosamine deacetylase

Reaction: UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamine + H2O = UDP-3-O-[(3R)-3-hydroxymyristoyl]-α-D-glucosamine + acetate

Other name(s): LpxC protein; LpxC enzyme; LpxC deacetylase; deacetylase LpxC; UDP-3-O-acyl-GlcNAc deacetylase; UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-acyl)-N-acetylglucosamine deacetylase; UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase; UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase

For diagram of reaction click here.

Systematic name: UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase

Comments: A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280 (2005) 16969-16978. [PMID: 15705580]

2. Jackman, J.E., Raetz, C.R. and Fierke, C.A. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 38 (1999) 1902-1911. [PMID: 10026271]

3. Hyland, S.A., Eveland, S.S. and Anderson, M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J. Bacteriol. 179 (1997) 2029-2037. [PMID: 9068651]

4. Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. Anal. Biochem. 290 (2001) 338-346. [PMID: 11237337]

5. Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 8146-8150. [PMID: 12819349]

6. Mochalkin, I., Knafels, J.D. and Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Sci. 17 (2008) 450-457. [PMID: 18287278]

[EC 3.5.1.108 created 2010]

EC 3.5.1.109

Accepted name: sphingomyelin deacylase

Reaction: (1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine

Glossary: sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide

Other name(s): SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase

Systematic name: N-acyl-sphingosylphosphorylcholine amidohydrolase

Comments: The enzyme is involved in the sphingolipid metabolism in the epidermis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406-413. [PMID: 10951276]

2. Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747-756. [PMID: 10970788]

3. Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397-408. [PMID: 12649340]

[EC 3.5.1.109 created 2011]

EC 3.5.1.110

Accepted name: peroxyureidoacrylate/ureidoacrylate amidohydrolase

Reaction: (1) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + CO2 + NH3 (overall reaction)
(1a) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + carbamate
(1b) carbamate = CO2 + NH3 (spontaneous)
(2) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + CO2 + NH3 (overall reaction)
(2a) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + carbamate
(2b) carbamate = CO2 + NH3 (spontaneous)

Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid

Other name(s): RutB

Systematic name: (Z)-3-ureidoacrylate peracid amidohydrolase

Comments: The enzyme also shows activity towards ureidoacrylate. Part of the Rut pyrimidine catabolic pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089-4102. [PMID: 20400551]

[EC 3.5.1.110 created 2012]

EC 3.5.1.111

Accepted name: 2-oxoglutaramate amidase

Reaction: 2-oxoglutaramate + H2O = 2-oxoglutarate + NH3

Glossary: 2-oxoglutaramate = 2-ketoglutaramate = 5-amino-2,5-dioxopentanoate

Other name(s): ω-amidase (ambiguous)

Systematic name: 5-amino-2,5-dioxopentanoate amidohydrolase

Comments: The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Cobzaru, C., Ganas, P., Mihasan, M., Schleberger, P. and Brandsch, R. Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res. Microbiol. 162 (2011) 285-291. [PMID: 21288482]

[EC 3.5.1.111 created 2012]

EC 3.5.1.112

Accepted name: 2'-N-acetylparomamine deacetylase

Reaction: 2'-N-acetylparomamine + H2O = paromamine + acetate

For diagram of reaction click here.

Glossary: paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine

Other name(s): btrD (gene name); neoL (gene name); kanN (gene name)

Systematic name: 2'-N-acetylparomamine hydrolase (acetate-forming)

Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2'''-acetyl-6'''-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2'''-acetyl-6'''-hydroxyneomycin C deacetylase [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew. Chem. Int. Ed. Engl. 46 (2007) 1462-1464. [PMID: 17226887]

2. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]

[EC 3.5.1.112 created 2012]

EC 3.5.1.113

Accepted name: 2'''-acetyl-6'''-hydroxyneomycin C deacetylase

Reaction: 2'''-acetyl-6'''-deamino-6'''-hydroxyneomycin C + H2O = 6'''-deamino-6'''-hydroxyneomycin C + acetate

For diagram of reaction click here.

Other name(s): neoL (gene name)

Systematic name: 2'''-acetyl-6'''-hydroxyneomycin C hydrolase (acetate-forming)

Comments: Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 3.5.1.112, 2'-N-acetylparomamine deacetylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem. 9 (2008) 865-869. [PMID: 18311744]

[EC 3.5.1.113 created 2012]

EC 3.5.1.114

Accepted name: N-acyl-aromatic-L-amino acid amidohydrolase

Reaction: (1) an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate
(2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate

Glossary: N-acetyl-L-cysteine-S-conjugate = mercapturic acid

Other name(s): aminoacylase 3; aminoacylase III; ACY3 (gene name)

Systematic name: N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)

Comments: This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nα-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Pushkin, A., Carpenito, G., Abuladze, N., Newman, D., Tsuprun, V., Ryazantsev, S., Motemoturu, S., Sassani, P., Solovieva, N., Dukkipati, R. and Kurtz, I. Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am. J. Physiol. Cell Physiol. 286 (2004) C848-C856. [PMID: 14656720]

2. Newman, D., Abuladze, N., Scholz, K., Dekant, W., Tsuprun, V., Ryazantsev, S., Bondar, G., Sassani, P., Kurtz, I. and Pushkin, A. Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. Drug Metab. Dispos. 35 (2007) 43-50. [PMID: 17012540]

3. Tsirulnikov, K., Abuladze, N., Newman, D., Ryazantsev, S., Wolak, T., Magilnick, N., Koag, M.C., Kurtz, I. and Pushkin, A. Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. Biochim. Biophys. Acta 1794 (2009) 1049-1057. [PMID: 19362172]

4. Hsieh, J.M., Tsirulnikov, K., Sawaya, M.R., Magilnick, N., Abuladze, N., Kurtz, I., Abramson, J. and Pushkin, A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc. Natl. Acad. Sci. USA 107 (2010) 17962-17967. [PMID: 20921362]

5. Tsirulnikov, K., Abuladze, N., Bragin, A., Faull, K., Cascio, D., Damoiseaux, R., Schibler, M.J. and Pushkin, A. Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal. Toxicol. Appl. Pharmacol. 263 (2012) 303-314. [PMID: 22819785]

[EC 3.5.1.114 created 2013]

EC 3.5.1.115

Accepted name: mycothiol S-conjugate amidase

Reaction: a mycothiol S-conjugate + H2O = an N-acetyl L-cysteine-S-conjugate + 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol

Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
N-acetyl L-cysteine-S-conjugate = mercapturic acid

Other name(s): MCA

Systematic name: mycothiol S-conjugate 1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranosyl-hydrolase

Comments: The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics. The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103, N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase) [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Newton, G.L., Av-Gay, Y. and Fahey, R.C. A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry 39 (2000) 10739-10746. [PMID: 10978158]

2. Steffek, M., Newton, G.L., Av-Gay, Y. and Fahey, R.C. Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. Biochemistry 42 (2003) 12067-12076. [PMID: 14556638]

[EC 3.5.1.115 created 2013]

EC 3.5.1.116

Accepted name: ureidoglycolate amidohydrolase

Reaction: (S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2

For diagram of reaction click here.

Other name(s): ureidoglycolate hydrolase; UAH (gene name)

Systematic name: (S)-ureidoglycolate amidohydrolase (decarboxylating)

Comments: This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 4.3.2.3, ureidoglycolate lyase, which releases urea rather than ammonia.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Winkler, R.G., Blevins, D.G. and Randall, D.D. Ureide catabolism in soybeans. III. Ureidoglycolate amidohydrolase and allantoate amidohydrolase are activities of an allantoate degrading enzyme complex. Plant Physiol. 86 (1988) 1084-1088. [PMID: 16666035]

2. Wells, X.E. and Lees, E.M. Ureidoglycolate amidohydrolase from developing French bean fruits (Phaseolus vulgaris [L.].). Arch. Biochem. Biophys. 287 (1991) 151-159. [PMID: 1910298]

3. Werner, A.K., Romeis, T. and Witte, C.P. Ureide catabolism in Arabidopsis thaliana and Escherichia coli. Nat. Chem. Biol. 6 (2010) 19-21. [PMID: 19935661]

[EC 3.5.1.116 created 1992 as EC 3.5.3.19, transferred 2014 to EC 3.5.1.116]

EC 3.5.1.117

Accepted name: 6-aminohexanoate-oligomer endohydrolase

Reaction: [N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x

Other name(s): endo-type 6-aminohexanoate oligomer hydrolase; Ahx endo-type-oligomer hydrolase; 6-aminohexanoate oligomer hydrolase; Ahx-oligomer hydrolase; nylon hydrolase; nylon-oligomer hydrolase; NylC; nylon-6 hydrolase (ambiguous)

Systematic name: 6-aminohexanoate oligomer endoamidohydrolase

Comments: The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear or cyclic oligomers of poly(6-aminohexanoate) with a degree of polymerization greater than three (n-> 3) by endo-type cleavage, to oligomers of a length of two or more (2 ≤ x-< n). It shows negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate (cf. EC 3.5.1.46, 6-aminohexanoate-oligomer exo hydrolase) or with 1,8-diazacyclotetradecane-2,9-dione (cf. EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kakudo, S., Negoro, S., Urabe, I. and Okada, H. Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product. Appl. Environ. Microbiol. 59 (1993) 3978-3980. [PMID: 8285701]

2. Yasuhira, K., Tanaka, Y., Shibata, H., Kawashima, Y., Ohara, A., Kato, D., Takeo, M. and Negoro, S. 6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2. Appl. Environ. Microbiol. 73 (2007) 7099-7102. [PMID: 17827307]

3. Negoro, S., Shibata, N., Tanaka, Y., Yasuhira, K., Shibata, H., Hashimoto, H., Lee, Y.H., Oshima, S., Santa, R., Oshima, S., Mochiji, K., Goto, Y., Ikegami, T., Nagai, K., Kato, D., Takeo, M. and Higuchi, Y. Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis. J. Biol. Chem. 287 (2012) 5079-5090. [PMID: 22187439]

[EC 3.5.1.117 created 2014]

EC 3.5.1.118

Accepted name: γ-glutamyl hercynylcysteine S-oxide hydrolase

Reaction: γ-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = S-(hercyn-2-yl)-L-cysteine S-oxide + L-glutamate

For diagram of reaction click here.

Glossary: hercynine = Nα,Nα,Nα-trimethyl-L-histidine = 3-(1H-imidazol-5-yl)-2-(trimethylamino)propanoate
S-(hercyn-2-yl)-L-cysteine S-oxide = S-(N,N,N-trimethyl-L-histidin-2-yl)-L-cysteine S-oxide

Other name(s): EgtC

Systematic name: γ-glutamyl-S-(hercyn-2-yl)cysteine S-oxide amidohydrolase

Comments: The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Seebeck, F.P. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632-6633. [PMID: 20420449]

[EC 3.5.1.118 created 2015]

EC 3.5.1.119

Accepted name: Pup amidohydrolase

Reaction: [prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3

Other name(s): dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase

Systematic name: [prokaryotic ubiquitin-like protein]-L-glutamine amidohydrolase

Comments: The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis.The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Striebel, F., Imkamp, F., Sutter, M., Steiner, M., Mamedov, A. and Weber-Ban, E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 16 (2009) 647-651. [PMID: 19448618]

2. Burns, K.E., Cerda-Maira, F.A., Wang, T., Li, H., Bishai, W.R. and Darwin, K.H. "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. Mol. Cell 39 (2010) 821-827. [PMID: 20705495]

3. Striebel, F., Imkamp, F., Özcelik, D. and Weber-Ban, E. Pupylation as a signal for proteasomal degradation in bacteria. Biochim. Biophys. Acta 1843 (2014) 103-113. [PMID: 23557784]

[EC 3.5.1.119 created 2015]

[EC 3.5.1.120 Transferred entry: 2-aminomuconate deaminase (2-hydroxymuconate-forming). Now EC 3.5.99.11, 2-aminomuconate deaminase (2-hydroxymuconate-forming) (EC 3.5.1.120 created 2016, deleted 2017)]

EC 3.5.1.121

Accepted name: protein N-terminal asparagine amidohydrolase

Reaction: N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3

Other name(s): NTAN1 (gene name)

Systematic name: protein N-terminal asparagine amidohydrolase

Comments: This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Stewart, A.E., Arfin, S.M. and Bradshaw, R.A. Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme. J. Biol. Chem. 269 (1994) 23509-23517. [PMID: 8089117]

2. Grigoryev, S., Stewart, A.E., Kwon, Y.T., Arfin, S.M., Bradshaw, R.A., Jenkins, N.A., Copeland, N.G. and Varshavsky, A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271 (1996) 28521-28532. [PMID: 8910481]

3. Cantor, J.R., Stone, E.M. and Georgiou, G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry 50 (2011) 3025-3033. [PMID: 21375249]

[EC 3.5.1.121 created 2016]

EC 3.5.1.122

Accepted name: protein N-terminal glutamine amidohydrolase

Reaction: N-terminal L-glutaminyl-[protein] + H2O = N-terminal L-glutamyl-[protein] + NH3

Other name(s): NTAQ1 (gene name)

Systematic name: protein N-terminal glutamine amidohydrolase

Comments: This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Gln. Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wang, H., Piatkov, K.I., Brower, C.S. and Varshavsky, A. Glutamine-specific N-terminal amidase, a component of the N-end rule pathway. Mol. Cell 34 (2009) 686-695. [PMID: 19560421]

[EC 3.5.1.122 created 2016]

EC 3.5.1.123

Accepted name: γ-glutamylanilide hydrolase

Reaction: N5-phenyl-L-glutamine + H2O = L-glutamate + aniline

Glossary: γ-glutamylanilide = N5-phenyl-L-glutamine

Other name(s): atdA2 (gene name)

Systematic name: N5-phenyl-L-glutamine amidohydrolase

Comments: The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the opposite reaction from that cayalysed by EC 6.3.1.18, γ-glutamylanilide synthase, which is part of an aniline degradation pathway. Its purpose is likely to maintain a low concentration of N5-phenyl-L-glutamine, which is potentially toxic.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Takeo, M., Ohara, A., Sakae, S., Okamoto, Y., Kitamura, C., Kato, D. and Negoro, S. Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. J. Bacteriol. 195 (2013) 4406-4414. [PMID: 23893114]

[EC 3.5.1.123 created 2016]

EC 3.5.1.124

Accepted name: protein deglycase

Reaction: (1) an Nω-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + (R)-lactate
(2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + (R)-lactate
(3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + (R)-lactate

Glossary: 2-oxopropanal = methylglyoxal

Other name(s): PARK7 (gene name); DJ-1 protein; yhbO (gene name); yajL (gene name); glyoxylase III (incorrect)

Systematic name: a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]

Comments: The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Misra, K., Banerjee, A.B., Ray, S. and Ray, M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem. J. 305 (1995) 999-1003. [PMID: 7848303]

2. Subedi, K.P., Choi, D., Kim, I., Min, B. and Park, C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol. Microbiol. 81 (2011) 926-936. [PMID: 21696459]

3. Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T. and Lamouri, A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290 (2015) 1885-1897. [PMID: 25416785]

4. Mihoub, M., Abdallah, J., Gontero, B., Dairou, J. and Richarme, G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463 (2015) 1305-1310. [PMID: 26102038]

5. Abdallah, J., Mihoub, M., Gautier, V. and Richarme, G. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 470 (2016) 282-286. [PMID: 26774339]

[EC 3.5.1.124 created 2016]

EC 3.5.1.125

Accepted name: N2-acetyl-L-2,4-diaminobutanoate deacetylase

Reaction: N2-acetyl-L-2,4-diaminobutanoate + H2O = L-2,4-diaminobutanoate + acetate

Other name(s): doeB (gene name)

Systematic name: N2-acetyl-L-2,4-diaminobutanoate amidohydrolase

Comments: The enzyme, found in bacteria, has no activity with N4-acetyl-L-2,4-diaminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase).

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Schwibbert, K., Marin-Sanguino, A., Bagyan, I., Heidrich, G., Lentzen, G., Seitz, H., Rampp, M., Schuster, S.C., Klenk, H.P., Pfeiffer, F., Oesterhelt, D. and Kunte, H.J. A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T. Environ. Microbiol. 13 (2011) 1973-1994. [PMID: 20849449]

[EC 3.5.1.125 created 2017]

EC 3.5.1.126

Accepted name: oxamate amidohydrolase

Reaction: oxamate + H2O = oxalate + NH3

Other name(s): HpxW

Systematic name: oxamate amidohydrolase

Comments: The enzyme has been characterized from the bacterium Klebsiella pneumoniae.

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Hicks, K.A. and Ealick, S.E. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol 72 (2016) 808-816. [PMID: 27303801]

[EC 3.5.1.126 created 2017]

EC 3.5.1.127

Accepted name: jasmonoyl-L-amino acid hydrolase

Reaction: a jasmonoyl-L-amino acid + H2O = jasmonate + an L-amino acid

Glossary: tuberonic acid = 12-hydroxyjasmonate = {(1R,2R)-3-oxo-2-[(2Z)-5-hydroxypent-2-enyl]cyclopentyl}acetate
jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-enyl]cyclopentyl}acetate

Other name(s): IAR3 (gene name); ILL4 (gene name); ILL6 (gene name)

Systematic name: jasmonoyl-L amino acid amidohydrolase

Comments: This entry includes a family of enzymes that recyle jasmonoyl-amino acid conjugates back to jasmonates. The enzymes from Arabidopsis thaliana have been shown to also act on 12-hydroxyjasmonoyl-L-isoleucine, generating tuberonic acid.

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Widemann, E., Miesch, L., Lugan, R., Holder, E., Heinrich, C., Aubert, Y., Miesch, M., Pinot, F. and Heitz, T. The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in Arabidopsis leaves. J. Biol. Chem. 288 (2013) 31701-31714. [PMID: 24052260]

[EC 3.5.1.127 created 2017]

EC 3.5.1.128

Accepted name: deaminated glutathione amidase

Reaction: N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine

Glossary: N-(4-oxoglutaryl)-L-cysteinylglycine = deaminated glutathione

Other name(s): dGSH deaminase; NIT1 (gene name)

Systematic name: N-(4-oxoglutaryl)-L-cysteinylglycine amidohydrolase

Comments: The enzyme, present in animals, fungi and bacteria, is involved in clearing cells of the toxic compound deaminated glutathione, which can be produced as an unwanted side product by several transaminases.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Peracchi, A., Veiga-da-Cunha, M., Kuhara, T., Ellens, K.W., Paczia, N., Stroobant, V., Seliga, A.K., Marlaire, S., Jaisson, S., Bommer, G.T., Sun, J., Huebner, K., Linster, C.L., Cooper, A.JL. and Van Schaftingen, E. Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione. Proc. Natl Acad. Sci. USA 114 (2017) E3233-E3242. [PMID: 28373563]

[EC 3.5.1.128 created 2018]

EC 3.5.1.129

Accepted name: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine hydrolase

Reaction: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine + H2O = cytidine 5'-diphosphoramidate + L-glutamate

Other name(s): N5-(cytidine 5'-diphosphoramidyl)-L-glutamine deacylase

Systematic name: N5-(cytidine 5'-diphosphoramidyl)-L-glutamine amidohydrolase

Comments: The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Taylor, Z.W., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079-6082. [PMID: 29023101]

[EC 3.5.1.129 created 2018]

EC 3.5.1.130

Accepted name: [lysine-biosynthesis-protein LysW]-lysine/ornithine hydrolase

Reaction: (1) [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-ornithyl)-L-glutamate + H2O = [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-ornithine
(2) [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-lysyl)-L-glutamate + H2O = [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-lysine

Other name(s): lysK (gene name)

Systematic name: [lysine-biosynthesis-protein LysW]-C-terminal-γ-(L-ornithyl/L-lysyl)-L-glutamate amidohydrolase

Comments: The enzyme participates in L-arginine and L-lysine biosynthetic pathways in certain species of archaea and bacteria. In some organisms the enzyme also catalyses the activity of EC 3.5.1.132, [amino group carrier protein]-ornithine hydrolase.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673-679. [PMID: 19620981]

[EC 3.5.1.130 created 2019]

EC 3.5.1.131

Accepted name: 1-carboxybiuret hydrolase

Reaction: 1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3

For diagram of reaction click here.

Glossary: carboxybiuret = carbamoylcarbamoylcarbamic acid

Other name(s): atzEG (gene names)

Systematic name: 1-carboxybiuret amidohydrolase

Comments: The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem 293 (2018) 7880-7891. [PMID: 29523689]

[EC 3.5.1.131 created 2019]

EC 3.5.1.132

Accepted name: [amino group carrier protein]-ornithine hydrolase

Reaction: [amino group carrier protein]-C-terminal-γ-(L-ornithyl)-L-glutamate + H2O = [amino group carrier protein]-C-terminal-L-glutamate + L-ornithine

Other name(s): lysK (gene name)

Systematic name: [amino group carrier protein]-C-terminal-γ-L-ornithyl-L-glutamate amidohydrolase

Comments: The enzyme participates in an L-arginine biosynthetic pathways in certain species of archaea and bacteria. In all cases known so far the enzyme also catalyses the activity of EC 3.5.1.130, [amino group carrier protein]-lysine hydrolase.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277-283. [PMID: 23434852]

2. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]

[EC 3.5.1.132 created 2019]


Continued with EC 3.5.2.1 to EC 3.5.3.21
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page