Enzyme Nomenclature

Continued from EC 3.5.1.51 to EC 3.5.1.132

EC 3.5.2 and EC 3.5.3

Sections

EC 3.5.2 In Cyclic Amides
EC 3.5.3 In Linear Amidines


EC 3.5.2 In Cyclic Amides

Contents

EC 3.5.2.1 barbiturase
EC 3.5.2.2 dihydropyrimidinase
EC 3.5.2.3 dihydroorotase
EC 3.5.2.4 carboxymethylhydantoinase
EC 3.5.2.5 allantoinase
EC 3.5.2.6 β-lactamase
EC 3.5.2.7 imidazolonepropionase
EC 3.5.2.8 deleted, included in EC 3.5.2.6
EC 3.5.2.9 5-oxoprolinase (ATP-hydrolysing)
EC 3.5.2.10 creatininase
EC 3.5.2.11 L-lysine-lactamase
EC 3.5.2.12 6-aminohexanoate-cyclic-dimer hydrolase
EC 3.5.2.13 2,5-dioxopiperazine hydrolase
EC 3.5.2.14 N-methylhydantoinase (ATP-hydrolysing)
EC 3.5.2.15 cyanuric acid amidohydrolase
EC 3.5.2.16 maleimide hydrolase
EC 3.5.2.17 hydroxyisourate hydrolase
EC 3.5.2.18 enamidase
EC 3.5.2.19 streptothricin hydrolase
EC 3.5.2.20 isatin hydrolase


Entries

EC 3.5.2.1

Accepted name: barbiturase

Reaction: barbiturate + H2O = 3-oxo-3-ureidopropanoate

For diagram, click here

Glossary: barbiturate = 6-hydroxyuracil

Systematic name: barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)

Comments: Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-16-5

References:

1. Hayaishi, O. and Kornberg, A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J. Biol. Chem. 197 (1952) 717-723. [PMID: 12981104]

2. 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]

3. 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 3.5.2.1 created 1961, modified 2006]

EC 3.5.2.2

Accepted name: dihydropyrimidinase

Reaction: 5,6-dihydrouracil + H2O = 3-ureidopropanoate

For diagram of reaction click here.

Other name(s): hydantoinase; hydropyrimidine hydrase; hydantoin peptidase; pyrimidine hydrase; D-hydantoinase

Systematic name: 5,6-dihydropyrimidine amidohydrolase

Comments: Also acts on dihydrothymine and hydantoin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-74-4

References:

1. Brooks, K.P., Jones, E.A., Kim, B.-D. and Sander, E.G. Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. Arch. Biochem. Biophys. 226 (1983) 469-483. [PMID: 6639068]

2. Eadie, G.S., Bernheim, F. and Bernheim, J.L.C. Metabolism of cytosine, thymidine, uracil and barbituric acid by bacterial enzymes. J. Biol. Chem. 181 (1949) 449-458. [PMID: 15393763]

[EC 3.5.2.2 created 1961]

EC 3.5.2.3

Accepted name: dihydroorotase

Reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate

For diagram click here.

Other name(s): carbamoylaspartic dehydrase; dihydroorotate hydrolase

Systematic name: (S)-dihydroorotate amidohydrolase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9024-93-5

References:

1. Cooper, C. and Wilson, D.W. Biosynthesis of pyrimidines. Fed. Proc. 13 (1954) 194 only.

2. Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911-924.

[EC 3.5.2.3 created 1961]

EC 3.5.2.4

Accepted name: carboxymethylhydantoinase

Reaction: L-5-carboxymethylhydantoin + H2O = N-carbamoyl-L-aspartate

Other name(s): hydantoin hydrolase

Systematic name: L-5-carboxymethylhydantoin amidohydrolase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9025-14-3

References:

1. Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911-924.

[EC 3.5.2.4 created 1961]

EC 3.5.2.5

Accepted name: allantoinase

Reaction: (S)-allantoin + H2O = allantoate

For diagram click here.

Systematic name: (S)-allantoin amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-20-1

References:

1. Florkin, M. and Duchateau-Bosson, G. Microdosage photométrique de l'allantoïne en solutions pures et dans l'urine. Enzymologia 9 (1940) 5-9.

[EC 3.5.2.5 created 1961]

EC 3.5.2.6

Accepted name: β-lactamase

Reaction: A β-lactam + H2O = a substituted β-amino acid

For diagram click here.

Other name(s): penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase

Systematic name: β-lactam hydrolase

Comments: A group of enzymes of varying specificity hydrolysing β-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9073-60-3

References:

1. Citri, N. Penicillinase and other β-lactamases, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 4, Academic Press, New York, 1971, pp. 23-46.

2. Hennessey, T.D. and Richmond, M.H. The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae. Biochem. J. 109 (1968) 469-473. [PMID: 5685878]

3. Kuwabara, S. Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H. Biochem. J. 118 (1970) 457-465. [PMID: 4990588]

4. Pollock, M.R. Penicillinase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 269-278.

5. Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. Crystalline bacterial penicillinase. Biochem. J. 62 (1956) 387-391.

6. Ross, G.W. and Boulton, M.G. Purification of β-lactamases on QAE-sephadex. Biochim. Biophys. Acta 309 (1973) 430-439. [PMID: 4731970]

[EC 3.5.2.6 created 1961, modified 1981 (EC 3.5.2.8 created 1972, incorporated 1978)]

EC 3.5.2.7

Accepted name: imidazolonepropionase

Reaction: (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+

For diagram click here.

Other name(s): 4(5)-imidazolone-5(4)-propionic acid hydrolase; imidazolone propionic acid hydrolase

Systematic name: 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-91-3

References:

1. Rao, D.R. and Greenberg, D.M. Studies on the enzymic decomposition of urocanic acid. IV. Purification and properties of 4(5)-imidazolone-5(4)-propionic acid hydrolase. J. Biol. Chem. 236 (1961) 1758-1763.

2. Snyder, S.H., Silva, O.L. and Kies, M.W. The mammalian metabolism of L-histidine. IV. Purification and properties of imidazolone propionic acid hydrolase. J. Biol. Chem. 236 (1961) 2996-2998.

[EC 3.5.2.7 created 1965, modified 2001]

[EC 3.5.2.8 Deleted entry: cephalosporinase. Now included with EC 3.5.2.6 β-lactamase (EC 3.5.2.8 created 1972, deleted 1978)]

EC 3.5.2.9

Accepted name: 5-oxoprolinase (ATP-hydrolysing)

Reaction: ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate

Other name(s): pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase

Systematic name: 5-oxo-L-proline amidohydrolase (ATP-hydrolysing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-46-1

References:

1. van der Werf, P., Orlowski, M. and Meister, A. Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the γ-glutamyl cycle. Proc. Natl. Acad. Sci. USA 68 (1971) 2982-2985. [PMID: 5289242]

[EC 3.5.2.9 created 1976]

EC 3.5.2.10

Accepted name: creatininase

Reaction: creatinine + H2O = creatine

Other name(s): creatinine hydrolase

Systematic name: creatinine amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-13-2

References:

1. Tsuru, D., Oka, I. and Yoshimoto, T. Creatinine decomposing enzymes in Pseudomonas putida. Agric. Biol. Chem. 40 (1976) 1011-1018.

[EC 3.5.2.10 created 1978]

EC 3.5.2.11

Accepted name: L-lysine-lactamase

Accepted name: L-lysine-lactamase

Reaction: (S)-2-aminohexano-6-lactam + H2O = L-lysine

Glossary: (S)-2-aminohexano-6-lactam = L-lysine 1,6-lactam

Other name(s): L-α-aminocaprolactam hydrolase; L-lysinamidase; L-lysine-1,6-lactam lactamhydrolase

Systematic name: (S)-2-aminohexano-6-lactam lactamhydrolase

Comments: Also hydrolyses L-lysinamide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52652-61-6

References:

1. Fukumura, T., Talbot, G., Misono, H., Teremura, Y., Kato, K. and Soda, K. Purification and properties of a novel enzyme, L-α-amino-ε-caprolactamase from Cryptococcus laurentii. FEBS Lett. 89 (1978) 298-300. [PMID: 26602]

2. Shvyadas, V.K., Galaev, I.Yu. and Kozlova, E.V. Preparation and characterization of L-α-aminocaprolactam hydrolase from cells of Cryptococcus laurentii. Biochemistry (Moscow) 49 (1984) 1268-1273.

[EC 3.5.2.11 created 1981, modified 1989]

EC 3.5.2.12

Accepted name: 6-aminohexanoate-cyclic-dimer hydrolase

Reaction: 1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate

Systematic name: 1,8-diazacyclotetradecane-2,9-dione lactamhydrolase

Comments: The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 60976-29-6

References:

1. Kinoshita, S., Negoro, S., Muramatsu, M., Bisaria, V.S., Sawada, S. and Okada, H. 6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI74. Eur. J. Biochem. 80 (1977) 489-495. [PMID: 923591]

[EC 3.5.2.12 created 1983]

EC 3.5.2.13

Accepted name: 2,5-dioxopiperazine hydrolase

Reaction: 2,5-dioxopiperazine + H2O = glycylglycine

Other name(s): cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase

Systematic name: 2,5-dioxopiperazine amidohydrolase

Comments: Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97599-45-6

References:

1. Suzuki, Y. and Uchida, K. Multiple forms of α-glycosidase from pig duodenum. Agric. Biol. Chem. 49 (1985) 1573-1581.

[EC 3.5.2.13 created 1989]

EC 3.5.2.14

Accepted name: N-methylhydantoinase (ATP-hydrolysing)

Reaction: ATP + N-methylhydantoin + 2 H2O = ADP + phosphate + N-carbamoylsarcosine

For diagram of reaction click here.

Glossary: N-methylhydantoin = N-methylimidazolidine-2,4-dione

Other name(s): N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing)

Systematic name: N-methylhydantoin amidohydrolase (ATP-hydrolysing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 100785-00-0

References:

1. Kim, J.M., Shimizu, S. and Yamada, H. Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis. Biochem. Biophys. Res. Commun. 142 (1987) 1006-1012. [PMID: 3827889]

[EC 3.5.2.14 created 1989]

EC 3.5.2.15

Accepted name: cyanuric acid amidohydrolase

Reaction: cyanuric acid + H2O = 1-carboxybiuret

For diagram of reaction click here.

Glossary: cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine
1-carboxybiuret = N-[(carbamoylamino)carbonyl]carbamate

Other name(s): atzD (gene name); trzD (gene name)

Systematic name: cyanuric acid amidohydrolase

Comments: The enzyme catalyses the ring cleavage 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 enzyme is highly specific for cyanuric acid. The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, UM-BBD, CAS registry number: 132965-78-7

References:

1. Eaton, R.W. and Karns, J.S. Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains. J. Bacteriol. 173 (1991) 1363-1366. [PMID: 1991731]

2. Eaton, R.W. and Karns, J.S. Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. J. Bacteriol. 173 (1991) 1215-1222. [PMID: 1846859]

3. Karns, J.S. Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227. Appl. Environ. Microbiol. 65 (1999) 3512-3517. [PMID: 10427042]

4. Fruchey, I., Shapir, N., Sadowsky, M.J. and Wackett, L.P. On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP. Appl. Environ. Microbiol. 69 (2003) 3653-3657. [PMID: 12788776]

5. 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 3.5.2.15 created 2000, modified 2008, modified 2019]

EC 3.5.2.16

Accepted name: maleimide hydrolase

Reaction: maleimide + H2O = maleamic acid

Other name(s): imidase; cyclic imide hydrolase; cyclic-imide amidohydrolase (decyclicizing) [misprint]; cyclic-imide amidohydrolase (decyclizing)

Systematic name: cyclic-imide amidohydrolase (ring-opening)

Comment: Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-74-4

References:

1. Ogawa, J., Soong, C.L., Honda, M. and Shimizu, S. Imidase, a new dihydropyrimidinase-like enzyme involved in the metabolism of cyclic imides. Eur. J. Biochem. 243 (1997) 322-327. [PMID: 9030755]

[EC 3.5.2.16 created 2001]

EC 3.5.2.17

Accepted name: hydroxyisourate hydrolase

Reaction: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate

For diagram click here.

Other name(s): HIUHase; 5-hydroxyisourate hydrolase

Systematic name: 5-hydroxyisourate amidohydrolase

Comments: The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 255885-20-2

References:

1. Raychaudhuri, A. and Tipton, P.A. A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase. Biochemistry 42 (2003) 6848-6852.[PMID: 12779339]

2. Raychaudhuri, A. and Tipton, P.A. Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism. Plant Physiol. 130 (2002) 2061-2068. [PMID: 12481089]

3. Sarma, A.D., Serfozo, P., Kahn, K. and Tipton, P.A. Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J. Biol. Chem. 274 (1999) 33863-33865. [PMID: 10567345]

[EC 3.5.2.17 created 2004]

EC 3.5.2.18

Accepted name: enamidase

Reaction: 6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3

For diagram click here.

Systematic name: 6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase

Comments: Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).

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

References:

1. Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341-12346. [PMID: 16894175]

[EC 3.5.2.18 created 2006]

EC 3.5.2.19

Accepted name: streptothricin hydrolase

Reaction: streptothricin-F + H2O = streptothricin-F acid

Other name(s): sttH (gene name)

Systematic name: streptothricin-F hydrolase

Comments: The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid [1]. The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei [1,2].

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

References:

1. Maruyama, C. and Hamano, Y. The biological function of the bacterial isochorismatase-like hydrolase SttH. Biosci. Biotechnol. Biochem. 73 (2009) 2494-2500. [PMID: 19897889]

2. Hamano, Y., Matsuura, N., Kitamura, M. and Takagi, H. A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific. J. Biol. Chem. 281 (2006) 16842-16848. [PMID: 16641084]

[EC 3.5.2.19 created 2011]

EC 3.5.2.20

Accepted name: isatin hydrolase

Reaction: isatin + H2O = isatinate

Glossary: isatin = 1H-indole-2,3-dione
isatinate = 2-(2-aminophenyl)-2-oxoacetate

Systematic name: isatin amidohydrolase

Comments: Requires Mn2+. This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.

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

References:

1. Sommer, M.R. and Jochimsen, B. Identification of enzymes involved in indole-3-acetic acid degradation. Plant Soil 186 (1996) 143-149.

2. Bjerregaard-Andersen, K., Sommer, T., Jensen, J.K., Jochimsen, B., Etzerodt, M. and Morth, J.P. A proton wire and water channel revealed in the crystal structure of isatin hydrolase. J. Biol. Chem. 289 (2014) 21351-21359. [PMID: 24917679]

[EC 3.5.2.20 created 2014]


EC 3.5.3 In Linear Amidines

Contents

EC 3.5.3.1 arginase
EC 3.5.3.2 guanidinoacetase
EC 3.5.3.3 creatinase
EC 3.5.3.4 allantoicase
EC 3.5.3.5 formiminoaspartate deiminase
EC 3.5.3.6 arginine deiminase
EC 3.5.3.7 guanidinobutyrase
EC 3.5.3.8 formiminoglutamase
EC 3.5.3.9 allantoate deiminase
EC 3.5.3.10 D-arginase
EC 3.5.3.11 agmatinase
EC 3.5.3.12 agmatine deiminase
EC 3.5.3.13 formiminoglutamate deiminase
EC 3.5.3.14 amidinoaspartase
EC 3.5.3.15 protein-arginine deiminase
EC 3.5.3.16 methylguanidinase
EC 3.5.3.17 guanidinopropionase
EC 3.5.3.18 dimethylargininase
EC 3.5.3.19 transferred now EC 3.5.1.116
EC 3.5.3.20 diguanidinobutanase
EC 3.5.3.21 methylenediurea deaminase
EC 3.5.3.22 proclavaminate amidinohydrolase
EC 3.5.3.23 N-succinylarginine dihydrolase
EC 3.5.3.24 N1-aminopropylagmatine ureohydrolase
EC 3.5.3.25 Nω-hydroxy-L-arginine amidinohydrolase
EC 3.5.3.26 (S)-ureidoglycine aminohydrolase


Entries

EC 3.5.3.1

Accepted name: arginase

Reaction: L-arginine + H2O = L-ornithine + urea

For diagram click here.

Other name(s): arginine amidinase; canavanase; L-arginase; arginine transamidinase

Systematic name: L-arginine amidinohydrolase

Comments: Also hydrolyses α-N-substituted L-arginines and canavanine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9000-96-8

References:

1. Bach, S.J. and Killip, J.D. Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver.Biochim. Biophys. Acta 47 (1961) 336-343.

2. Cabello, J., Basilio, C. and Prajoux, V. Kinetic properties of erythrocyte- and liver arginase. Biochim. Biophys. Acta 48 (1961) 148-152.

3. Dumitru, I.F. Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight. Acta Vitamin. Enzymol. 27 (1973) 207-210.

4. Greenberg, D.M. Arginase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 257-267.

5. Greenberg, D.M., Bagot, A.E. and Roholt, O.A. Liver arginase. III. Properties of highly purified arginase. Arch. Biochem. Biophys. 62 (1956) 446-453.

[EC 3.5.3.1 created 1961]

EC 3.5.3.2

Accepted name: guanidinoacetase

Reaction: guanidinoacetate + H2O = glycine + urea

Other name(s): glycocyaminase

Systematic name: guanidinoacetate amidinohydrolase

Comments: Requires Mn2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-92-4

References:

1. Roche, J., Lacombe, G. and Girard, H. Sur la spécificité de certaines déguanidases bactériennes génératrices d'urée et sur l'argininedihydrolase. Biochim. Biophys. Acta 6 (1950) 210-216.

2. Yorifuji, T., Tamai, H. and Usami, H. Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas. Agric. Biol. Chem. 41 (1977) 959-966.

[EC 3.5.3.2 created 1961]

EC 3.5.3.3

Accepted name: creatinase

Reaction: creatine + H2O = sarcosine + urea

For diagram of reaction click here.

Systematic name: creatine amidinohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37340-58-2

References:

1. Roche, J., Lacombe, G. and Girard, H. Sur la spécificité de certaines déguanidases bactériennes génératrices d'urée et sur l'argininedihydrolase. Biochim. Biophys. Acta 6 (1950) 210-216.

2. Yoshimoto, T., Oka, I. and Tsuru, D. Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida. J. Biochem. (Tokyo) 79 (1976) 1381-1383. [PMID: 8443]

[EC 3.5.3.3 created 1961]

EC 3.5.3.4

Accepted name: allantoicase

Reaction: allantoate + H2O = (S)-ureidoglycolate + urea

For diagram click here.

Systematic name: allantoate amidinohydrolase

Comments: Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-21-2

References:

1. Florkin, M. and Duchateau-Bosson, G. Microdosage photométrique de l'allantoïne en solutions pures et dans l'urine. Enzymologia 9 (1940) 5-9.

2. Trijbels, F. and Vogels, G.D. Allantoicase and ureidoglycolase in Pseudomonas and Penicillium species. Biochim. Biophys. Acta 118 (1966) 387-395. [PMID: 4960174]

3. van der Drift, C. and Vogels, G.D. Effect of metal and hydrogen ions on the activity and stability of allantoicase. Biochim. Biophys. Acta 198 (1971) 339-352.

4. s'Gravenmade, E.J., van der Drift, C. and Vogels, G.D. Hydrolysis, racemization and absolute configuration of ureidoglycolate, a substrate of allantoicase. Biochim. Biophys. Acta 198 (1971) 569-582.

[EC 3.5.3.4 created 1961]

EC 3.5.3.5

Accepted name: formimidoylaspartate deiminase

Reaction:N-formimidoyl-L-aspartate + H2O = N-formyl-L-aspartate + NH3

Other name(s): formiminoaspartate deiminase

Systematic name:N-formimidoyl-L-aspartate iminohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-07-4

References:

1. Hayaishi, O., Tabor, H. and Hayaishi, T. N-Formimino-L-aspartic acid as an intermediate in the enzymic conversion of imidazoleacetic acid to formylaspartic acid. J. Biol. Chem. 227 (1957) 161-180.

[EC 3.5.3.5 created 1961, modified 2000]

EC 3.5.3.6

Accepted name: arginine deiminase

Reaction: L-arginine + H2O = L-citrulline + NH3

Other name(s): arginine dihydrolase; citrulline iminase; L-arginine deiminase

Systematic name: L-arginine iminohydrolase

Comments: Also acts on canavanine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-98-9

References:

1. Oginsky, E.L. and Gehrig, R.F. The arginine dihydrolase system of Streptococcus faecalis. II. Properties of arginine desimidase. J. Biol. Chem. 198 (1952) 799-805.

2. Petrack, B., Sullivan, L. and Ratner, S. Behavior of purified arginine desiminase from S. faecalis. Arch. Biochem. Biophys. 69 (1957) 186-197.

3. Ratner, S. Urea synthesis and metabolism of arginine and citrulline. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 319-387.

[EC 3.5.3.6 created 1961]

EC 3.5.3.7

Accepted name: guanidinobutyrase

Reaction: 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea

For diagram, click here

Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA

Other name(s): γ-guanidobutyrase; 4-guanidinobutyrate amidinobutyrase; γ-guanidinobutyrate amidinohydrolase; G-Base; GBH; guanidinobutyrate ureahydrolase

Systematic name: 4-guanidinobutanoate amidinohydrolase

Comments: Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidinohexanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9013-69-8

References:

1. Mora, J., Tarrab, R., Martuscelli, J. and Soberón, G. Characteristics of arginases from ureotelic and non-ureotelic animals. Biochem. J. 96 (1965) 588-594. [PMID: 5862400]

2. Thoai, N.V., Thome-Beau, F. and Olomucki, A. [Induction and specificity of enzymes of the new catabolic arginine pathway]. Biochim. Biophys. Acta 115 (1966) 73-80. [PMID: 5936244]

3. Yorifuji, T., Kato, M., Kobayashi, T., Ozaki, S. and Ueno, S. 4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties. Agric. Biol. Chem. 44 (1980) 1127-1134.

4. Yorifuji, T., Kobayashi, T., Tabuchi, A., Shiritani, Y. and Yonaha, K. Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping. Agric. Biol. Chem. 47 (1983) 2825-2830.

[EC 3.5.3.7 created 1972]

EC 3.5.3.8

Accepted name: formimidoylglutamase

Reaction: N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide

For diagram click here.

Other name(s): formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase

Systematic name: N-formimidoyl-L-glutamate formimidoylhydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9054-92-6

References:

1. Kaminskas, E., Kimhi, Y. and Magasanik, B. Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. J. Biol. Chem. 245 (1970) 3536-3544. [PMID: 4990470]

2. Lund, P. and Magasanik, B. N-Formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes. J. Biol. Chem. 240 (1965) 4316-4319. [PMID: 5845833]

[EC 3.5.3.8 created 1972, modified 2000, modified 2001]

EC 3.5.3.9

Accepted name: allantoate deiminase

Reaction: allantoate + H2O = (S)-ureidoglycine + NH3 + CO2

For diagram click here.

Other name(s): allantoate amidohydrolase

Systematic name: allantoate amidinohydrolase (decarboxylating)

Comments: This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-13-7

References:

1. Vogels, G.D. Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme. Biochim. Biophys. Acta 113 (1966) 277-291. [PMID: 5328936]

2. Serventi, F., Ramazzina, I., Lamberto, I., Puggioni, V., Gatti, R. and Percudani, R. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. ACS Chem Biol 5 (2010) 203-214. [PMID: 20038185]

[EC 3.5.3.9 created 1972, modified 2010]

EC 3.5.3.10

Accepted name: D-arginase

Reaction: D-arginine + H2O = D-ornithine + urea

Systematic name: D-arginine amidinohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-14-8

References:

1. Nadai, Y. Arginase. II. Distribution and properties of D-arginase. J. Biochem. (Tokyo) 45 (1958) 1011-1020.

[EC 3.5.3.10 created 1972]

EC 3.5.3.11

Accepted name: agmatinase

Reaction: agmatine + H2O = putrescine + urea

For diagram click here.

Glossary: agmatine = (4-aminobutyl)guanidine

Other name(s): agmatine ureohydrolase; SpeB

Systematic name: agmatine amidinohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-16-0

References:

1. Hirshfeld, I.N., Rosenfeld, H.J., Leifer, Z. and Maas, W.K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J. Bacteriol. 101 (1970) 725-730. [PMID: 4908780]

2. Vicente, C. and Legaz, M.E. Preparation and properties of agmatine amidinohydrolase of Evernia prunastri. Physiol. Plant. 55 (1982) 335-339.

[EC 3.5.3.11 created 1972]

EC 3.5.3.12

Accepted name: agmatine deiminase

Reaction: agmatine + H2O = N-carbamoylputrescine + NH3

Glossary: agmatine = (4-aminobutyl)guanidine

Other name(s): agmatine amidinohydrolase

Systematic name: agmatine iminohydrolase

Comments: The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-17-1

References:

1. Smith, T.A. Agmatine iminohydrolase in maize. Phytochemistry 8 (1969) 2111-2117.

2. Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532-9541. [PMID: 6895223]

[EC 3.5.3.12 created 1972]

EC 3.5.3.13

Accepted name: formimidoylglutamate deiminase

Reaction:N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3

For diagram click here.

Other name(s): formiminoglutamate deiminase; formiminoglutamic iminohydrolase

Systematic name:N-formimidoyl-L-glutamate iminohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-85-7

References:

1. Wickner, R.B. and Tabor, H. N-Formimino-L-glutamate iminohydrolase (Pseudomonas sp.). Methods Enzymol. 17B (1971) 80-84.

[EC 3.5.3.13 created 1975, modified 2000]

EC 3.5.3.14

Accepted name: amidinoaspartase

Reaction: N-amidino-L-aspartate + H2O = L-aspartate + urea

Other name(s): amidinoaspartic amidinohydrolase

Systematic name: N-amidino-L-aspartate amidinohydrolase

Comments: Also acts slowly on N-amidino-L-glutamate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37325-60-3

References:

1. Milstien S. and Goldman, P. Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis. J. Biol. Chem. 247 (1972) 6280-6283. [PMID: 4651648]

[EC 3.5.3.14 created 1976]

EC 3.5.3.15

Accepted name: protein-arginine deiminase

Reaction: protein L-arginine + H2O = protein L-citrulline + NH3

Other name(s): peptidylarginine deiminase; PAD

Systematic name: protein-L-arginine iminohydrolase

Comments: Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 75536-80-0

References:

1. Fujisaki, M. and Sugawara, K. Properties of peptidylarginine deiminase from the epidermis of newborn rats. J. Biochem. (Tokyo) 89 (1981) 257-263. [PMID: 7217033]

[EC 3.5.3.15 created 1983]

EC 3.5.3.16

Accepted name: methylguanidinase

Reaction: methylguanidine + H2O = methylamine + urea

Other name(s): methylguanidine hydrolase

Systematic name: methylguanidine amidinohydrolase

Comments: Acts on some other alkylguanidines, but very slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73200-93-8

References:

1. Nakajima, M., Shirokane, Y. and Mizusawa, K. A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42. FEBS Lett. 110 (1980) 43-46. [PMID: 7353662]

[EC 3.5.3.16 created 1984]

EC 3.5.3.17

Accepted name: guanidinopropionase

Reaction: 3-guanidinopropanoate + H2O = β-alanine + urea

Other name(s): GPase; GPH

Systematic name: 3-guanidinopropanoate amidinopropionase

Comments: Requires Mn2+. Also acts, more slowly, on taurocyamine and 4-guanidinobutanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68821-77-2

References:

1. Yorifuji, T., Sugai, I., Matsumoto, H. and Tabuchi, A. Characterization of 3-guanidinopropionate amidinohydrolase from Pseudomonas aeruginosa and a comparative study with 4- guanidinobutyrate amidinohydrolase from another Pseudomonas. Agric. Biol. Chem. 46 (1982) 1361-1363.

[EC 3.5.3.17 created 1989]

EC 3.5.3.18

Accepted name: dimethylargininase

Reaction: Nω,Nω'-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline

Other name(s): dimethylarginine dimethylaminohydrolase; NG,NG-dimethylarginine dimethylaminohydrolase; NG,NG-dimethyl-L-arginine dimethylamidohydrolase; ω,ω-di-N-methyl-L-arginine dimethylamidohydrolase

Systematic name: Nω,Nω'-dimethyl-L-arginine dimethylamidohydrolase

Comments: Also acts on Nω-methyl-L-arginine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 123644-75-7

References:

1. Ogawa, T., Kimoto, M. and Sasaoka, K. Purification and properties of a new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase, from rat kidney. J. Biol. Chem. 264 (1989) 10205-10209. [PMID: 2722865]

[EC 3.5.3.18 created 1992]

[EC 3.5.3.19 Transferred entry: ureidoglycolate hydrolase. Now classified as EC 3.5.1.116, ureidoglycolate amidohydrolase (EC 3.5.3.19 created 1992, deleted 2013)]

EC 3.5.3.20

Accepted name: diguanidinobutanase

Reaction: 1,4-diguanidinobutane + H2O = agmatine + urea

Glossary: agmatine = (4-aminobutyl)guanidine

Systematic name: 1,4-diguanidinobutane amidinohydrolase

Comments: Other diguanidinoalkanes with 3 to 10 methylene groups can also act, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125268-65-7

References:

1. Yorifuji, T., Kaneoke, M., Shimizu, E., Shiota, K. and Matsuo, R. Degradation of α,ω-diguanidinoalkanes and a novel enzyme, diguanidinobutane amidohydrolase, in Pseudomonas putida. Agric. Biol. Chem. 53 (1989) 3003-3009.

[EC 3.5.3.20 created 1992]

EC 3.5.3.21

Accepted name: methylenediurea deaminase

Reaction: (1a) NH2-CO-NH-CH2-NH-CO-NH2 + H2O = N-(carboxyaminomethyl)urea + NH3

(1b) N-(carboxyaminomethyl)urea = N-(aminomethyl)urea + CO2 (spontaneous)

(1c) N-(aminomethyl)urea + H2O = N-(hydroxymethyl)urea + NH3 (spontaneous)

Other name(s): methylenediurease

Systematic name: methylenediurea aminohydrolase

Comments: The methylenediurea is hydrolysed and decarboxylated to give an aminated methylurea, which then spontaneously hydrolyses to hydroxymethylurea. The enzyme from Ochrobactrum anthropi also hydrolyses dimethylenetriurea and trimethylenetetraurea as well as ureidoglycolate, which is hydrolysed to urea and glyoxylate, and allantoate, which is hydrolysed to ureidoglycolate, ammonia and carbon dioxide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 205830-62-2

References:

1. Jahns, T., Schepp, R., Kaltwasser, H. Purification and characterisation of an enzyme from a strain of Ochrobactrum anthropi that degrades condensation products of urea and formaldehyde (ureaform). Can. J. Microbiol. 43 (1997) 1111-1117.

[EC 3.5.3.21 created 1999]

EC 3.5.3.22

Accepted name: proclavaminate amidinohydrolase

Reaction: amidinoproclavaminate + H2O = proclavaminate + urea

For diagram click here.

Other name(s): PAH; proclavaminate amidino hydrolase

Systematic name: amidinoproclavaminate amidinohydrolase

Comments: Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme. Requires Mn2+.

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

References:

1. Salowe, S.P., Krol, W.J., Iwatareuyl, D. and Townsend, C.A. Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. Biochemistry 30 (1991) 2281-2292. [PMID: 1998687]

2. Zhou, J., Kelly, W.L., Bachmann, B.O., Gunsior, M., Townsend, C.A. and Solomon, E.I. Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities. J. Am. Chem. Soc. 123 (2001) 7388-7389.

3. Townsend, C.A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6 (2002) 583-589. [PMID: 12413541]

4. Wu, T.K., Busby, R.W., Houston, T.A., McIlwaine, D.B., Egan, L.A. and Townsend, C.A. Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis. J. Bacteriol. 177 (1995) 3714-3720. [PMID: 7601835]

[EC 3.5.3.22 created 2003]

EC 3.5.3.23

Accepted name: N-succinylarginine dihydrolase

Reaction: N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2

For diagram, click here

Other name(s): N2-succinylarginine dihydrolase; arginine succinylhydrolase; SADH; AruB; AstB

Systematic name: N2-succinyl-L-arginine iminohydrolase (decarboxylating)

Comments: Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second 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 2.6.1.81 (succinylornithine 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:

References:

1. 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]

2. Tocilj, A., Schrag, J.D., Li, Y., Schneider, B.L., Reitzer, L., Matte, A. and Cygler, M. Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. J. Biol. Chem. 280 (2005) 15800-15808. [PMID: 15703173]

3. 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]

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

5. 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]

[EC 3.5.3.23 created 2006]

EC 3.5.3.24

Accepted name: N1-aminopropylagmatine ureohydrolase

Reaction: N1-aminopropylagmatine + H2O = spermidine + urea

For diagram of reaction click here.

Systematic name: N1-aminopropylagmatine amidinohydrolase

Comments: The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine.

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

References:

1. Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E. and Oshima, T. N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus. J. Biol. Chem. 280 (2005) 30073-30082. [PMID: 15983049]

2. Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T. and Fujiwara, S. Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 192 (2010) 4991-5001. [PMID: 20675472]

[EC 3.5.3.24 created 2013]

EC 3.5.3.25

Accepted name: Nω-hydroxy-L-arginine amidinohydrolase

Reaction: Nω-hydroxy-L-arginine + H2O = L-ornithine + hydroxyurea

Other name(s): dcsB (gene name)

Systematic name: Nω-hydroxy-L-arginine amidinohydrolase

Comments: The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.

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

References:

1. Kumagai, T., Koyama, Y., Oda, K., Noda, M., Matoba, Y. and Sugiyama, M. Molecular cloning and heterologous expression of a biosynthetic gene cluster for the antitubercular agent D-cycloserine produced by Streptomyces lavendulae. Antimicrob. Agents Chemother. 54 (2010) 1132-1139. [PMID: 20086163]

2. Kumagai, T., Takagi, K., Koyama, Y., Matoba, Y., Oda, K., Noda, M. and Sugiyama, M. Heme protein and hydroxyarginase necessary for biosynthesis of D-cycloserine. Antimicrob. Agents Chemother. 56 (2012) 3682-3689. [PMID: 22547619]

[EC 3.5.3.25 created 2013]

EC 3.5.3.26

Accepted name: (S)-ureidoglycine aminohydrolase

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

For diagram click here.

Other name(s): UGlyAH; UGHY; ylbA (gene name)

Systematic name: (S)-ureidoglycine aminohydrolase

Comments: Binds Mn2+. This enzyme, found in plants and bacteria, is part of the ureide pathway, which enables the recycling of the nitrogen in purine compounds. In plants it is localized in the endoplasmic reticulum.

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

References:

1. Serventi, F., Ramazzina, I., Lamberto, I., Puggioni, V., Gatti, R. and Percudani, R. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. ACS Chem. Biol. 5 (2010) 203-214. [PMID: 20038185]

2. 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]

3. Shin, I., Percudani, R. and Rhee, S. Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana. J. Biol. Chem. 287 (2012) 18796-18805. [PMID: 22493446]

[EC 3.5.3.26 created 2013]


Continued with EC 3.5.4.1 to EC 3.5.99.2
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