Enzyme Nomenclature

EC 4.1.1 (continued)

Carboxy-Lyases

Continued from EC 4.1.1.1 to EC 4.1.1.50

Contents

EC 4.1.1.51 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase
EC 4.1.1.52 6-methylsalicylate decarboxylase
EC 4.1.1.53 phenylalanine decarboxylase
EC 4.1.1.54 dihydroxyfumarate decarboxylase
EC 4.1.1.55 4,5-dihydroxyphthalate decarboxylase
EC 4.1.1.56 3-oxolaurate decarboxylase
EC 4.1.1.57 methionine decarboxylase
EC 4.1.1.58 orsellinate decarboxylase
EC 4.1.1.59 gallate decarboxylase
EC 4.1.1.60 stipitatonate decarboxylase
EC 4.1.1.61 4-hydroxybenzoate decarboxylase
EC 4.1.1.62 gentisate decarboxylase
EC 4.1.1.63 protocatechuate decarboxylase
EC 4.1.1.64 2,2-dialkylglycine decarboxylase (pyruvate)
EC 4.1.1.65 phosphatidylserine decarboxylase
EC 4.1.1.66 uracil-5-carboxylate decarboxylase
EC 4.1.1.67 UDP-galacturonate decarboxylase
EC 4.1.1.68 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
EC 4.1.1.69 3,4-dihydroxyphthalate decarboxylase
EC 4.1.1.70 glutaconyl-CoA decarboxylase
EC 4.1.1.71 2-oxoglutarate decarboxylase
EC 4.1.1.72 branched-chain-2-oxoacid decarboxylase
EC 4.1.1.73 tartrate decarboxylase
EC 4.1.1.74 indolepyruvate decarboxylase
EC 4.1.1.75 5-guanidino-2-oxopentanoate decarboxylase
EC 4.1.1.76 arylmalonate decarboxylase
EC 4.1.1.77 2-oxo-3-hexenedioate decarboxylase
EC 4.1.1.78 acetylenedicarboxylate decarboxylase
EC 4.1.1.79 sulfopyruvate decarboxylase
EC 4.1.1.80 4-hydroxyphenylpyruvate decarboxylase
EC 4.1.1.81 threonine-phosphate decarboxylase
EC 4.1.1.82 phosphonopyruvate decarboxylase
EC 4.1.1.83 4-hydroxyphenylacetate decarboxylase
EC 4.1.1.84 D-dopachrome decarboxylase
EC 4.1.1.85 3-dehydro-L-gulonate-6-phosphate decarboxylase
EC 4.1.1.86 diaminobutyrate decarboxylase
EC 4.1.1.87 malonyl-S-ACP decarboxylase
EC 4.1.1.88 biotin-independent malonate decarboxylase
EC 4.1.1.89 now EC 7.2.4.4
EC 4.1.1.90 peptidyl-glutamate 4-carboxylase
EC 4.1.1.91 salicylate decarboxylase
EC 4.1.1.92 indole-3-carboxylate decarboxylase
EC 4.1.1.93 pyrrole-2-carboxylate decarboxylase
EC 4.1.1.94 ethylmalonyl-CoA decarboxylase
EC 4.1.1.95 L-glutamyl-[BtrI acyl-carrier protein] decarboxylase
EC 4.1.1.96 carboxynorspermidine decarboxylase
EC 4.1.1.97 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
EC 4.1.1.98 4-hydroxy-3-polyprenylbenzoate decarboxylase
EC 4.1.1.99 phosphomevalonate decarboxylase
EC 4.1.1.100 prephenate decarboxylase
EC 4.1.1.101 malolactic enzyme
EC 4.1.1.102 phenacrylate decarboxylase
EC 4.1.1.103 γ-resorcylate decarboxylase
EC 4.1.1.104 3-dehydro-4-phosphotetronate decarboxylase
EC 4.1.1.105 L-tryptophan decarboxylase
EC 4.1.1.106 fatty acid photodecarboxylase
EC 4.1.1.107 3,4-dihydroxyphenylacetaldehyde synthase
EC 4.1.1.108 4-hydroxyphenylacetaldehyde synthase
EC 4.1.1.109 phenylacetaldehyde synthase
EC 4.1.1.110 bisphosphomevalonate decarboxylase
EC 4.1.1.111 siroheme decarboxylase
EC 4.1.1.112 oxaloacetate decarboxylase
EC 4.1.1.113 trans-aconitate decarboxylase
EC 4.1.1.114 cis-3-alkyl-4-alkyloxetan-2-one decarboxylase

Entries

EC 4.1.1.51

Accepted name: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase

Reaction: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate = 3-hydroxy-2-methylpyridine-5-carboxylate + CO2

For diagram of reaction click here.

Systematic name: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37289-49-9

References:

1. Snell, E.E., Smucker, A.A., Ringelmann, E. and Lynen, F. Die bakterielle Oxydation des Vitamin B6. IV. Die enzymatische Decarboxylierung von 2-Methyl-3-hydroxypyridine-4,5-dicarbonsäure. Biochem. Z. 341 (1964) 109-119.

[EC 4.1.1.51 created 1972]

EC 4.1.1.52

Accepted name: 6-methylsalicylate decarboxylase

Reaction: 6-methylsalicylate = 3-methylphenol + CO2

Glossary: 3-methylphenol = 3-cresol = m-cresol

Other name(s): 6-methylsalicylic acid (2,6-cresotic acid) decarboxylase; 6-MSA decarboxylase; 6-methylsalicylate carboxy-lyase

Systematic name: 6-methylsalicylate carboxy-lyase (3-methylphenol-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-50-2

References:

1. Light, R.J. 6-Methylsalicylic acid decarboxylase from Penicillium patulum. Biochim. Biophys. Acta 191 (1969) 430-438. [PMID: 5354271]

2. Vogel, G. and Lynen, F. 6-Methylsalicylsäure-Decarboxylase. Naturwissenschaften 57 (1970) 664.

[EC 4.1.1.52 created 1972, modified 2011]

EC 4.1.1.53

Accepted name: phenylalanine decarboxylase

Reaction: L-phenylalanine = phenylethylamine + CO2

Other name(s): L-phenylalanine decarboxylase; aromatic L-amino acid decarboxylase

Systematic name: L-phenylalanine carboxy-lyase

Comments: A pyridoxal-phosphate protein. Also acts on tyrosine and other aromatic amino acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9075-72-3

References:

1. Lovenberg, W., Weissbach, H. and Udenfriend, S. Aromatic L-amino acid decarboxylase. J. Biol. Chem. 237 (1962) 89-93.

2. Schulz, A.R. and Oliner, L. The possible role of thyroid aromatic amino acid decarboxylase in thyroxine biosynthesis. Life Sci. 6 (1967) 873-880. [PMID: 6034195]

[EC 4.1.1.53 created 1972]

EC 4.1.1.54

Accepted name: dihydroxyfumarate decarboxylase

Reaction: dihydroxyfumarate = 2-hydroxy-3-oxopropanoate + CO2

Glossary: 2-hydroxy-3-oxopropanoate = tartronate semialdehyde

Other name(s): dihydroxyfumarate carboxy-lyase

Systematic name: dihydroxyfumarate carboxy-lyase (2-hydroxy-3-oxopropanoate-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-51-3

References:

1. Fukumaga, K. Metabolism of dihydroxyfumarate, hydroxypyruvate, and their related compounds. I. Enzymic formation of xylulose in liver. J. Biochem. (Tokyo) 47 (1960) 741-754.

[EC 4.1.1.54 created 1972]

EC 4.1.1.55

Accepted name: 4,5-dihydroxyphthalate decarboxylase

Reaction: 4,5-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2

Systematic name: 4,5-dihydroxyphthalate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37290-48-5

References:

1. Ribbons, D.W. and Evans, W.C. Oxidative metabolism of phthalic acid by soil pseudomonads. Biochem. J. 76 (1966) 310-318.

[EC 4.1.1.55 created 1972]

EC 4.1.1.56

Accepted name: 3-oxolaurate decarboxylase

Reaction: 3-oxododecanoate = 2-undecanone + CO2

Other name(s): β-ketolaurate decarboxylase; β-ketoacyl decarboxylase

Systematic name: 3-oxododecanoate carboxy-lyase

Comments: Also decarboxylates other C14 to C16 oxo acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-49-6

References:

1. Franke, W., Platzeck, A. and Eichhorn, G. [On the knowledge of fatty acid catabolism by mold fungi. III. On a decarboxylase for average β-ketomonocarbonic acids (β-ketolaurate decarboxylase)] Arch. Mikrobiol. 40 (1961) 73-93.

[EC 4.1.1.56 created 1972]

EC 4.1.1.57

Accepted name: methionine decarboxylase

Reaction: L-methionine = 3-(methylsulfanyl)propanamine + CO2

Other name(s): L-methionine decarboxylase

Systematic name: L-methionine carboxy-lyase [3-(methylsulfanyl)propanamine-forming]; L-methionine carboxy-lyase (3-methylthiopropanamine-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-50-9

References:

1. Hagion, H. and Nakayama, K. Amino acid metabolism in microorganisms. Part IV. L-Methionine decarboxylase produced by Streptomyces strain. Agric. Biol. Chem. 32 (1968) 727-733.

[EC 4.1.1.57 created 1972]

EC 4.1.1.58

Accepted name: orsellinate decarboxylase

Reaction: orsellinate = orcinol + CO2

Glossary: orsellinate = 2,4-dihydroxy-6-methylbenzoate

Other name(s): orsellinate carboxy-lyase

Systematic name: 2,4-dihydroxy-6-methylbenzoate carboxy-lyase (orcinol-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-58-8

References:

1. Pettersson, G. An orsellinic acid decarboxylase isolated from Gliocladium roseum. Acta Chem. Scand. 19 (1965) 2013-2021.

[EC 4.1.1.58 created 1972]

EC 4.1.1.59

Accepted name: gallate decarboxylase

Reaction: 3,4,5-trihydroxybenzoate = pyrogallol + CO2

Glossary: gallate = 3,4,5-trihydroxybenzoate

Other name(s): gallic acid decarboxylase; gallate carboxy-lyase

Systematic name: 3,4,5-trihydroxybenzoate carboxy-lyase (pyrogallol-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37290-51-0

References:

1. Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325-343.

[EC 4.1.1.59 created 1972]

EC 4.1.1.60

Accepted name: stipitatonate decarboxylase

Reaction: stipitatonate = stipitatate + CO2

Other name(s): stipitatonate carboxy-lyase (decyclizing); stipitatonate carboxy-lyase (decyclizing, stipitatate-forming)

Systematic name: stipitatonate carboxy-lyase (ring-opening, stipitatate-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-52-1

References:

1. Bentley, R. and Thiessen, C.P. Biosynthesis of tropolones in Penicillium stipitatum. V. Preparation and properties of stipitatonic acid decarboxylase. J. Biol. Chem. 238 (1963) 3811-3816.

[EC 4.1.1.60 created 1972]

EC 4.1.1.61

Accepted name: 4-hydroxybenzoate decarboxylase

Reaction: 4-hydroxybenzoate = phenol + CO2

Other name(s): p-hydroxybenzoate decarboxylase

Systematic name: 4-hydroxybenzoate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37290-53-2

References:

1. Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325-343.

2. Tschech, A. and Fuchs, G. Anaerobic degradation of phenol via carboxylation to 4-hydroxybenzoate - in vitro study of isotope exchange between (CO2)-C-14 and 4-hydroxybenzoate. Arch. Microbiol. 152 (1989) 594-599.

[EC 4.1.1.61 created 1972]

EC 4.1.1.62

Accepted name: gentisate decarboxylase

Reaction: 2,5-dihydroxybenzoate = hydroquinone + CO2

Glossary: gentisate = 2,5-dihydroxybenzoate

Other name(s): 2,5-dihydroxybenzoate decarboxylase; gentisate carboxy-lyase

Systematic name: 2,5-dihydroxybenzoate carboxy-lyase (hydroquinone-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37290-54-3

References:

1. Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325-343.

[EC 4.1.1.62 created 1972]

EC 4.1.1.63

Accepted name: protocatechuate decarboxylase

Reaction: 3,4-dihydroxybenzoate = catechol + CO2

Glossary: protocatechuate = 3,4-dihydroxybenzoate

Other name(s): 3,4-dihydrobenzoate decarboxylase; protocatechuate carboxy-lyase

Systematic name: 3,4-dihydroxybenzoate carboxy-lyase (catechol-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37290-55-4

References:

1. Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325-343.

[EC 4.1.1.63 created 1972]

EC 4.1.1.64

Accepted name: 2,2-dialkylglycine decarboxylase (pyruvate)

Reaction: 2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine

Other name(s): dialkyl amino acid (pyruvate) decarboxylase; α-dialkyl amino acid transaminase; 2,2-dialkyl-2-amino acid-pyruvate aminotransferase; L-alanine-α-ketobutyrate aminotransferase; dialkylamino-acid decarboxylase (pyruvate); 2,2-dialkylglycine carboxy-lyase (amino-transferring)

Systematic name: 2,2-dialkylglycine carboxy-lyase (amino-transferring; L-alanine-forming)

Comments: A pyridoxal-phosphate protein. Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2-methylbutanoate and 1-aminocyclopentanecarboxylate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-17-1

References:

1. Bailey, G.B. and Dempsey, W.B. Purification and properties of an α-dialkyl amino acid transaminase. Biochemistry 6 (1967) 1526-1533.

[EC 4.1.1.64 created 1972]

EC 4.1.1.65

Accepted name: phosphatidylserine decarboxylase

Reaction: phosphatidyl-L-serine = phosphatidylethanolamine + CO2

Other name(s): PS decarboxylase

Systematic name: phosphatidyl-L-serine carboxy-lyase

Comments: A pyridoxal-phosphate protein. In Escherichia coli, the prosthetic group is a pyruvoyl group.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-78-8

References:

1. Kanfer, J. and Kennedy, E.P. Metabolism and function of bacterial lipids. II. Biosynthesis of phospholipids in Escherichia coli. J. Biol. Chem. 239 (1964) 1720-1726.

2. Satre, M. and Kennedy, E.P. Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli. J. Biol. Chem. 253 (1978) 479-483. [PMID: 338609]

[EC 4.1.1.65 created 1976]

EC 4.1.1.66

Accepted name: uracil-5-carboxylate decarboxylase

Reaction: uracil 5-carboxylate = uracil + CO2

Other name(s): uracil-5-carboxylic acid decarboxylase

Systematic name: uracil-5-carboxylate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 59299-01-3

References:

1. Palmatier, R.D., McCroskey, R.P. and Abbott, M.T. The enzymatic conversion of uracil 5-carboxylic acid to uracil and carbon dioxide. J. Biol. Chem. 245 (1970) 6706-6710. [PMID: 5482775]

[EC 4.1.1.66 created 1976]

EC 4.1.1.67

Accepted name: UDP-galacturonate decarboxylase

Reaction: UDP-D-galacturonate = UDP-L-arabinose + CO2

For diagram of reaction click here.

Other name(s): UDP-galacturonic acid decarboxylase; UDPGalUA carboxy lyase

Systematic name: UDP-D-galacturonate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9054-79-9

References:

1. Fan, D.-F. and Feingold, D.S. UDPgalacturonic acid decarboxylase from Ampullariella digitata. Methods Enzymol. 28B (1972) 438-439.

[EC 4.1.1.67 created 1984]

EC 4.1.1.68

Accepted name: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase

Reaction: (3E,5R)-5-carboxy-2-oxohept-3-enedioate = (4Z)-2-oxohept-4-enedioate + CO2 (overall reaction)
(1a) (3E,5R)-5-carboxy-2-oxohept-3-enedioate = (2Z,4Z)-2-hydroxyhepta-2,4-dienedioate + CO2
(1b) (2Z,4Z)-2-hydroxyhepta-2,4-dienedioate = (4Z)-2-oxohept-4-enedioate

Glossary: 5-carboxy-2-oxohept-3-enedioate = 5-oxopent-3-ene-1,2,5-tricarboxylate

Other name(s): 5-carboxymethyl-2-oxo-hex-3-ene-1,6-dioate decarboxylase

Systematic name: 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase

Comments: Requires Mg2+ [2,3]. Part of the 4-hydroxyphenylacetate degradation pathway in Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 148619-60-7 (151404-80-7 and 173015-33-3)

References:

1. Garrido-Pertierra, A. and Cooper, R.A. Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli. Eur. J. Biochem. 117 (1981) 581-584. [PMID: 7026235]

[EC 4.1.1.68 created 1984]

EC 4.1.1.69

Accepted name: 3,4-dihydroxyphthalate decarboxylase

Reaction: 3,4-dihydroxyphthalate = 3,4-dihydroxybenzoate + CO2

Systematic name: 3,4-dihydroxyphthalate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83137-76-2

References:

1. Eaton, R.W. and Ribbons, D.W. Metabolism of dibutylphthalate and phthalate by Micrococcus sp. strain 12B.J. Gen. Microbiol. 151 (1982) 48-57. [PMID: 7085570]

[EC 4.1.1.69 created 1986]

EC 4.1.1.70

Accepted name: glutaconyl-CoA decarboxylase

Reaction: 4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO2

Glossary: glutaconyl-CoA = 4-carboxybut-2-enoyl-CoA

Other name(s): glutaconyl coenzyme A decarboxylase; pent-2-enoyl-CoA carboxy-lyase

Systematic name: 4-carboxybut-2-enoyl-CoA carboxy-lyase

Comments: The enzyme from Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 84399-93-9

References:

1. Buckel, W.S. and Semmler, R. Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria. Eur. J. Biochem. 136 (1983) 427-434. [PMID: 6628393]

2. Buckel, W. Sodium ion-translocating decarboxylases. Biochim. Biophys. Acta 1505 (2001) 15-27. [PMID: 11248185]

[EC 4.1.1.70 created 1986, modified 2003]

EC 4.1.1.71

Accepted name: 2-oxoglutarate decarboxylase

Reaction: 2-oxoglutarate = succinate semialdehyde + CO2

For diagram of reaction click here.

Glossary: thiamine diphosphate

Other name(s): oxoglutarate decarboxylase; α-ketoglutarate decarboxylase; α-ketoglutaric decarboxylase; oxoglutarate decarboxylase; pre-2-oxoglutarate decarboxylase

Systematic name: 2-oxoglutarate carboxy-lyase

Comments: Requires thiamine diphosphate. Highly specific.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37205-42-8

References:

1. Shigeoka, S., Onishi, T., Maeda, K., Nakano, Y. and Kitaoka, S. Occurrence of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in mitochondria of Euglena gracilis. FEBS Lett. 195 (1986) 43-47.

[EC 4.1.1.71 created 1989]

EC 4.1.1.72

Accepted name: branched-chain-2-oxoacid decarboxylase

Reaction: (3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2

Other name(s): branched-chain oxo acid decarboxylase; branched-chain alpha-keto acid decarboxylase; branched-chain keto acid decarboxylase; BCKA

Systematic name: (3S)-3-methyl-2-oxopentanoate carboxy-lyase

Comments: Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 63653-19-0

References:

1. Oku, H. and Kaneda, T. Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase. J. Biol. Chem. 263 (1988) 18386-18396. [PMID: 3142877]

2. de la Plaza, M., Fernandez de Palencia, P., Pelaez, C. and Requena, T. Biochemical and molecular characterization of α-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis. FEMS Microbiol. Lett. 238 (2004) 367-374. [PMID: 15358422]

3. Smit, B.A., van Hylckama Vlieg, J.E., Engels, W.J., Meijer, L., Wouters, J.T. and Smit, G. Identification, cloning, and characterization of a Lactococcus lactis branched-chain α-keto acid decarboxylase involved in flavor formation. Appl. Environ. Microbiol. 71 (2005) 303-311. [PMID: 15640202]

[EC 4.1.1.72 created 1990]

EC 4.1.1.73

Accepted name: tartrate decarboxylase

Reaction: (R,R)-tartrate = D-glycerate + CO2

Systematic name: (R,R)-tartrate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 124248-30-2

References:

1. Furuyoshi, S., Kawabata, N., Tanaka, H. and Soda, K. Enzymatic production of D-glycerate from L-tartrate. Agric. Biol. Chem. 53 (1989) 2101-2105.

[EC 4.1.1.73 created 1992]

EC 4.1.1.74

Accepted name: indolepyruvate decarboxylase

Reaction: 3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2

Glossary: thiamine diphosphate

Other name(s): indol-3-yl-pyruvate carboxy-lyase; (indol-3-yl)pyruvate carboxy-lyase [(indol-3-yl)acetaldehyde-forming]

Systematic name: 3-(indol-3-yl)pyruvate carboxy-lyase [(2-indol-3-yl)acetaldehyde-forming]

Comments: Thiamine diphosphate- and Mg2+-dependent. More specific than EC 4.1.1.1 pyruvate decarboxylase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-92-4, 183213-32-3

References:

1. Koga, J. Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-pyruvic acid biosynthesis. Biochim. Biophys. Acta 1249 (1995) 1-13. [PMID: 7766676]

[EC 4.1.1.74 created 1999]

EC 4.1.1.75

Accepted name: 5-guanidino-2-oxopentanoate decarboxylase

Reaction: 5-guanidino-2-oxopentanoate = 4-guanidinobutanal + CO2

Glossary: thiamine diphosphate

Other name(s): α-ketoarginine decarboxylase; 5-guanidino-2-oxopentanoate carboxy-lyase

Systematic name: 5-guanidino-2-oxo-pentanoate carboxy-lyase (4-guanidinobutanal-forming)

Comments: enzyme activity is dependent on the presence of thiamine diphosphate and a divalent cation.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56831-67-5

References:

1. Vanderbilt, A.S., Gaby, N.S., Rodwell, V.W. Intermediates and enzymes between α-ketoarginine and γ-guanidinobutyrate in the L-arginine catabolic pathway of Pseudomonas putida. J. Biol. Chem. 250 (1975) 5322-5329. [PMID: 237915]

[EC 4.1.1.75 created 1999]

EC 4.1.1.76

Accepted name: arylmalonate decarboxylase

Reaction: 2-aryl-2-methylmalonate = 2-arylpropanoate + CO2

Other name(s): AMDASE; ; 2-aryl-2-methylmalonate carboxy-lyase; 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropionate-forming)

Systematic name: 2-aryl-2-methylmalonate carboxy-lyase (2-arylpropanoate-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 144713-36-0, 154102-95-1

References:

1. Miyamoto, K., Ohta, H. Cloning and heterologous expression of a novel arylmalonate decarboxylase gene from Alcaligenes bronchisepticus KU 1201. Appl. Microbiol. Biotechnol. 38 (1992) 234-238. [PMID: 1369144]

[EC 4.1.1.76 created 1999]

EC 4.1.1.77

Accepted name: 2-oxo-3-hexenedioate decarboxylase

Reaction: (3E)-2-oxohex-3-enedioate = 2-oxopent-4-enoate + CO2

For diagram of reaction click here.

Other name(s): 4-oxalocrotonate carboxy-lyase (misleading); 4-oxalocrotonate decarboxylase (misleading); cnbF (gene name); praD (gene name); amnE (gene name); nbaG (gene name); xylI (gene name)

Systematic name: (3E)-2-oxohex-3-enedioate carboxy-lyase (2-oxopent-4-enoate-forming)

Comments: Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. The enzyme has been reported to accept multiple tautomeric forms [1-4]. However, careful analysis of the stability of the different tautomers, as well as characterization of the enzyme that produces its substrate, EC 5.3.2.6, 2-hydroxymuconate tautomerase, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37325-55-6

References:

1. Shingler, V., Marklund, U., Powlowski, J. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174 (1992) 711-724. [PMID: 1732207]

2. Takenaka, S., Murakami, S., Shinke, R. and Aoki, K. Metabolism of 2-aminophenol by Pseudomonas sp. AP-3: modified meta-cleavage pathway. Arch. Microbiol. 170 (1998) 132-137. [PMID: 9683650]

3. Stanley, T.M., Johnson, W.H., Jr., Burks, E.A., Whitman, C.P., Hwang, C.C. and Cook, P.F. Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry 39 (2000) 718-726. [PMID: 10651637]

4. Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions. Biochemistry 46 (2007) 11919-11929. [PMID: 17902707]

5. Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758-6768. [PMID: 19717587]

[EC 4.1.1.77 created 1999, modified 2011, modified 2012]

EC 4.1.1.78

Accepted name: acetylenedicarboxylate decarboxylase

Reaction: acetylenedicarboxylate + H2O = pyruvate + CO2

Other name(s): acetylenedicarboxylate hydratase; acetylenedicarboxylate hydrase

Systematic name: acetylenedicarboxylate carboxy-lyase

Comments: The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate. It is thus analogous to EC 4.2.1.27 (acetylenecarboxylate hydratase) in its mechanism. Formerly EC 4.2.1.72

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72561-10-5

References:

1. Yamada, E.W. and Jakoby, W.B. Enzymatic utilization of acetylenic compounds. I. An enzyme converting acetylenedicarboxylic acid to pyruvate. J. Biol. Chem. 233 (1958) 706-711.

[EC 4.1.1.78 created 1978 as EC 4.2.1.72, transferred 2000 to EC 4.1.1.78]

EC 4.1.1.79

Accepted name: sulfopyruvate decarboxylase

Reaction: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO2

For diagram of reaction click here

Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
2-sulfoacetaldehyde = 2-oxoethanesulfonate

Other name(s): sulfopyruvate carboxy-lyase

Systematic name: 3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming)

Comments: Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 303155-97-7

References:

1. Graupner, M., Xu, H. and White, R.H. Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 182 (2000) 4862-4867. [PMID: 10940029]

[EC 4.1.1.79 created 2002]

EC 4.1.1.80

Accepted name: 4-hydroxyphenylpyruvate decarboxylase

Reaction: 4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO2

For diagram click here.

Systematic name: 4-hydroxyphenylpyruvate carboxy-lyase

Comments: Reacts with dopamine to give the benzylisoquinoline alkaloid skeleton.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 109300-96-1

References:

1. Rueffer, M. and Zenk, M.H. Distant precursors of benzylisoquinoline alkaloids and their enzymatic formation. Z. Naturforsch. C: Biosci. 42 (1987) 319-332.

[EC 4.1.1.80 created 2002]

EC 4.1.1.81

Accepted name: threonine-phosphate decarboxylase

Reaction: L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2

For diagram click here.

Other name(s): L-threonine-O-3-phosphate decarboxylase; CobD

Systematic name: L-threonine-O-3-phosphate carboxy-lyase

Comments: A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.

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

References:

1. Cheong, C.G., Bauer, C.B., Brushaber, K.R., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry 41 (2002) 4798-4808. [PMID: 11939774]

2. Brushaber, K.R., O'Toole, G.A. and Escalante-Semerena, J.C. CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. J. Biol. Chem. 273 (1998) 2684-2691. [PMID: 7559521]

3. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]

[EC 4.1.1.81 created 2004]

EC 4.1.1.82

Accepted name: phosphonopyruvate decarboxylase

Reaction: 3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2

For diagram of reaction click here.

Other name(s): 3-phosphonopyruvate carboxy-lyase

Systematic name: 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)

Comments: The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly. This enzyme drives the reaction catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the thermodynamically unfavourable direction of 3-phosphonopyruvate formation [2]. It is the initial step in all of the major biosynthetic pathways of phosphonate natural products [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 151662-34-9

References:

1. Zhang, G., Dai, J., Lu, Z. and Dunaway-Mariano, D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278 (2003) 41302-41308. [PMID: 12904299]

2. Seidel, H.M. and Knowles, J.R. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. Biochemistry 33 (1994) 5641-5646. [PMID: 8180189]

3. Nakashita, H., Watanabe, K., Hara, O., Hidaka, T. and Seto, H. Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate. J. Antibiot. (Tokyo) 50 (1997) 212-219. [PMID: 9127192]

[EC 4.1.1.82 created 2005]

EC 4.1.1.83

Accepted name: 4-hydroxyphenylacetate decarboxylase

Reaction: (4-hydroxyphenyl)acetate + H+ = 4-methylphenol + CO2

Other name(s): p-hydroxyphenylacetate decarboxylase; p-Hpd; 4-Hpd; 4-hydroxyphenylacetate carboxy-lyase

Systematic name: (4-hydroxyphenyl)acetate carboxy-lyase (4-methylphenol-forming)

Comments: The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 340137-18-0

References:

1. D'Ari, L., and Barker, H.A. p-Cresol formation by cell-free extracts of Clostridium difficile. Arch. Microbiol. 143 (1985) 311-312. [PMID: 3938267]

2. Selmer, T. and Andrei, P.I. p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol. Eur. J. Biochem. 268 (2001) 1363-1372. [PMID: 11231288]

3. Andrei, P.I., Pierik, A.J., Zauner, S., Andrei-Selmer, L.C. and Selmer, T. Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity. Eur. J. Biochem. 271 (2004) 2225-2230. [PMID: 15153112]

[EC 4.1.1.83 created 2005]

EC 4.1.1.84

Accepted name: D-dopachrome decarboxylase

Reaction: D-dopachrome = 5,6-dihydroxyindole + CO2

Glossary: D-dopachrome = (2R)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate

Other name(s): phenylpyruvate tautomerase II; D-tautomerase; D-dopachrome tautomerase; D-dopachrome carboxy-lyase

Systematic name: D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)

Comments: This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-α-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 184111-06-6

References:

1. Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H. Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole. Biochem. Biophys. Res. Commun. 197 (1993) 619-624. [PMID: 8267597]

2. Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K. NMR characterization of physicochemical properties of rat D-dopachrome tautomerase. Biochem. Mol. Biol. Int. 42 (1997) 891-899. [PMID: 9285056]

3. Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J. Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution. Biochemistry 38 (1999) 3268-3279. [PMID: 10079069]

4. Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M. Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation. Biochem. Biophys. Res. Commun. 243 (1998) 538-544. [PMID: 9480844]

[EC 4.1.1.84 created 2005]

EC 4.1.1.85

Accepted name: 3-dehydro-L-gulonate-6-phosphate decarboxylase

Reaction: 3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2

For diagram click here.

Other name(s): 3-keto-L-gulonate 6-phosphate decarboxylase; UlaD; SgaH; SgbH; KGPDC; 3-dehydro-L-gulonate-6-phosphate carboxy-lyase

Systematic name: 3-dehydro-L-gulonate-6-phosphate carboxy-lyase (L-xylulose-5-phosphate-forming)

Comments: Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.

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

References:

1. Yew, W.S. and Gerlt, J.A. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184 (2002) 302-306. [PMID: 11741871]

2. Wise, E., Yew, W.S., Babbitt, P.C., Gerlt, J.A. and Rayment, I. Homologous (β/α)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry 41 (2002) 3861-3869. [PMID: 11900527]

[EC 4.1.1.85 created 2005]

EC 4.1.1.86

Accepted name: diaminobutyrate decarboxylase

Reaction: L-2,4-diaminobutanoate = propane-1,3-diamine + CO2

For diagram, click here

Other name(s): DABA DC; L-2,4-diaminobutyrate decarboxylase; L-2,4-diaminobutanoate carboxy-lyase

Systematic name: L-2,4-diaminobutanoate carboxy-lyase (propane-1,3-diamine-forming)

Comments: A pyridoxal-phosphate protein that requires a divalent cation for activity [1]. 4-N-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate—2-oxoglutarate transaminase, which can supply the substrate for this enzyme.

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

References:

1.Yamamoto, S., Tsuzaki, Y., Tougou, K. and Shinoda, S. Purification and characterization of L-2,4-diaminobutyrate decarboxylase from Acinetobacter calcoaceticus. J. Gen. Microbiol. 138 (1992) 1461-1465. [PMID: 1512577]

2. Ikai, H. and Yamamoto, S. Cloning and expression in Escherichia coli of the gene encoding a novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter baumannii. FEMS Microbiol. Lett. 124 (1994) 225-228. [PMID: 7813892]

3. Ikai, H. and Yamamoto, S. Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J. Bacteriol. 179 (1997) 5118-5125. [PMID: 9260954]

[EC 4.1.1.86 created 2006]

EC 4.1.1.87

Accepted name: malonyl-S-ACP decarboxylase

Reaction: a malonyl-[acyl-carrier protein] + H+ = an acetyl-[acyl-carrier protein] + CO2

For diagram of the reaction click here

Other name(s): malonyl-S-acyl-carrier protein decarboxylase; MdcD/MdcE; MdcD,E

Systematic name: malonyl-[acyl-carrier-protein] carboxy-lyase

Comments: This enzyme comprises the β and γ subunits of EC 4.1.1.88 (biotin-independent malonate decarboxylase) but is not present in EC 4.1.1.89 (biotin-dependent malonate decarboxylase). It follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetylated form of the acyl-carrier-protein subunit of malonate decarboxylase [5]. The carboxy group is lost with retention of configuration [3].

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

References:

1. Schmid, M., Berg, M., Hilbi, H. and Dimroth, P. Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group. Eur. J. Biochem. 237 (1996) 221-228. [PMID: 8620876]

2. Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus<. Eur. J. Biochem. 266 (1999) 683-690. [PMID: 10561613]

3. Handa, S., Koo, J.H., Kim, Y.S. and Floss, H.G. Stereochemical course of biotin-independent malonate decarboxylase catalysis. Arch. Biochem. Biophys. 370 (1999) 93-96. [PMID: 10496981]

4. Chohnan, S., Akagi, K. and Takamura, Y. Functions of malonate decarboxylase subunits from Pseudomonas putida. Biosci. Biotechnol. Biochem. 67 (2003) 214-217. [PMID: 12619701]

5. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 4.1.1.87 created 2008]

EC 4.1.1.88

Accepted name: biotin-independent malonate decarboxylase

Reaction: malonate + H+ = acetate + CO2

For diagram of the reaction click here

Other name(s): malonate decarboxylase (without biotin); malonate decarboxylase (ambiguous); MDC

Systematic name: malonate carboxy-lyase (biotin-independent)

Comments: Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. This enzyme is a cytosolic protein that is biotin-independent. The other type is a biotin-dependent, Na+-translocating enzyme that includes both soluble and membrane-bound components (cf. EC 7.2.4.4, biotin-dependent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. In both enzymes, this is achieved by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-ACP. The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2-(5-triphosphoribosyl)-3-dephospho-CoA rather than as phosphopantetheine 4'-phosphate. The individual enzymes involved in carrying out the reaction of this enzyme complex are EC 2.3.1.187 (acetyl-S-ACP:malonate ACP transferase), EC 2.3.1.39 ([acyl-carrier-protein] S-malonyltransferase) and EC 4.1.1.87 (malonyl-S-ACP decarboxylase). The carboxy group is lost with retention of configuration [6].

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

References:

1. Schmid, M., Berg, M., Hilbi, H. and Dimroth, P. Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group. Eur. J. Biochem. 237 (1996) 221-228. [PMID: 8620876]

2. Byun, H.S. and Kim, Y.S. Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein. J. Biochem. Mol. Biol. 30 (1997) 132-137.

3. Hoenke, S., Schmid, M. and Dimroth, P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246 (1997) 530-538. [PMID: 9208947]

4. Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. Malonate decarboxylase of Pseudomonas putida is composed of five subunits. FEMS Microbiol. Lett. 169 (1998) 37-43. [PMID: 9851033]

5. Hoenke, S., Schmid, M. and Dimroth, P. Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases. Biochemistry 39 (2000) 13233-13240. [PMID: 11052676]

6. Handa, S., Koo, J.H., Kim, Y.S. and Floss, H.G. Stereochemical course of biotin-independent malonate decarboxylase catalysis. Arch. Biochem. Biophys. 370 (1999) 93-96. [PMID: 10496981]

7. Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem. 266 (1999) 683-690. [PMID: 10561613]

8. Kim, Y.S. Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application. J. Biochem. Mol. Biol. 35 (2002) 443-451. [PMID: 12359084]

9. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 4.1.1.88 created 2008, modified 2018]

[EC 4.1.1.89 Transferred entry: biotin-dependent malonate decarboxylase. Now EC 7.2.4.4, biotin-dependent malonate decarboxylase(EC 4.1.1.89 created 2008, deleted 2018)]

EC 4.1.1.90

Accepted name: peptidyl-glutamate 4-carboxylase

Reaction: peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinol

For diagram of reaction click here and mechanism click here.

Other name(s): vitamin K-dependent carboxylase; γ-glutamyl carboxylase; peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing)

Systematic name: peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinol-epoxidizing)

Comments: The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron. The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system. 9–12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein. The 4-pro-S hydrogen of the glutamate residue is removed [5] and there is an inversion of stereochemistry at this position [6].

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

References:

1. Dowd, P., Hershline, R., Ham, S.W. and Naganathan, S. Vitamin K and energy transduction: a base strength amplification mechanism. Science 269 (1995) 1684-1691. [PMID: 7569894]

2. Furie, B., Bouchard, B.A. and Furie, B.C. Vitamin K-dependent biosynthesis of γ-carboxyglutamic acid. Blood 93 (1999) 1798-1808. [PMID: 10068650]

3. Rishavy, M.A., Hallgren, K.W., Yakubenko, A.V., Shtofman, R.L., Runge, K.W. and Berkner, K.L. Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation. Biochemistry 45 (2006) 13239-13248. [PMID: 17073445]

4. Silva, P.J. and Ramos, M.J. Reaction mechanism of the vitamin K-dependent glutamate carboxylase: a computational study. J. Phys. Chem. B 111 (2007) 12883-12887. [PMID: 17935315]

[EC 4.1.1.90 created 2009]

EC 4.1.1.91

Accepted name: salicylate decarboxylase

Reaction: salicylate = phenol + CO2

Other name(s): salicylic acid decarboxylase; Scd

Systematic name: salicylate carboxy-lyase

Comments: In the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylate. The enzyme also catalyses the reversible decarboxylation of 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2,3-dihydroxybenzoate and 4-aminosalicylate [1].

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

References:

1. Kirimura, K., Gunji, H., Wakayama, R., Hattori, T. and Ishii, Y. Enzymatic Kolbe-Schmitt reaction to form salicylic acid from phenol: enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase. Biochem. Biophys. Res. Commun. 394 (2010) 279-284. [PMID: 20188702]

[EC 4.1.1.91 created 2011]

EC 4.1.1.92

Accepted name: indole-3-carboxylate decarboxylase

Reaction: indole-3-carboxylate = indole + CO2

Systematic name: indole-3-carboxylate carboxy-lyase

Comments: Activated by Zn2+, Mn2+ or Mg2+.

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

References:

1. Yoshida, T., Fujita, K. and Nagasawa, T. Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation. Biosci. Biotechnol. Biochem. 66 (2002) 2388-2394. [PMID: 12506977]

[EC 4.1.1.92 created 2011]

EC 4.1.1.93

Accepted name: pyrrole-2-carboxylate decarboxylase

Reaction: (1) pyrrole-2-carboxylate = pyrrole + CO2
(2) pyrrole-2-carboxylate + H2O = pyrrole + HCO3-

Systematic name: pyrrole-2-carboxylate carboxy-lyase

Comments: The enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide. The enzyme is activated by carboxylic acids.

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

References:

1. Wieser, M., Fujii, N., Yoshida, T. and Nagasawa, T. Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910. Eur. J. Biochem. 257 (1998) 495-499. [PMID: 9826198]

2. Omura, H., Wieser, M. and Nagasawa, T. Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme. Eur. J. Biochem. 253 (1998) 480-484. [PMID: 9654100]

3. Wieser, M., Yoshida, T. and Nagasawa, T. Microbial synthesis of pyrrole-2-carboxylate by Bacillus megaterium PYR2910. Tetrahedron Lett. 39 (1998) 4309-4310.

[EC 4.1.1.93 created 2011]

EC 4.1.1.94

Accepted name: ethylmalonyl-CoA decarboxylase

Reaction: (S)-ethylmalonyl-CoA = butanoyl-CoA + CO2

Systematic name: (S)-ethylmalonyl-CoA carboxy-lyase (butanoyl-CoA-forming)

Comments: The enzyme, which exists in all vertebrates, decarboxylates ethylmalonyl-CoA, a potentially toxic compound that is formed in low amounts by the activity of EC 6.4.1.2 (acetyl-CoA carboxylase) and EC 6.4.1.3 (propanoyl-CoA carboxylase). It prefers the S isomer, and can decarboxylate (R)-methylmalonyl-CoA with lower efficiency. cf. EC 7.2.4.1, (S)-methylmalonyl-CoA decarboxylase (sodium-transporting).

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

References:

1. Linster, C.L., Noel, G., Stroobant, V., Vertommen, D., Vincent, M.F., Bommer, G.T., Veiga-da-Cunha, M. and Van Schaftingen, E. Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite proofreading. J. Biol. Chem. 286 (2011) 42992-43003. [PMID: 22016388]

[EC 4.1.1.94 created 2012]

EC 4.1.1.95

Accepted name: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase

Reaction: L-glutamyl-[BtrI acyl-carrier protein] = 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2

Other name(s): btrK (gene name)

Systematic name: L-glutamyl-[BtrI acyl-carrier protein] carboxy-lyase

Comments: Binds pyridoxal 5'-phosphate. Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. Has very low activity with substrates not bound to an acyl-carrier protein.

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

References:

1. Li, Y., Llewellyn, N.M., Giri, R., Huang, F. and Spencer, J.B. Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway. Chem. Biol. 12 (2005) 665-675. [PMID: 15975512]

[EC 4.1.1.95 created 2012]

EC 4.1.1.96

Accepted name: carboxynorspermidine decarboxylase

Reaction: (1) carboxynorspermidine = bis(3-aminopropyl)amine + CO2
(2) carboxyspermidine = spermidine + CO2

Glossary: bis(3-aminopropyl)amine = norspermidine

Other name(s): carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name)

Systematic name: carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming)

Comments: A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3].

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

References:

1. Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899-9907. [PMID: 19196710]

2. Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and Phillips, M.A. Evolution of substrate specificity within a diverse family of β/α-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. J. Biol. Chem. 285 (2010) 25708-25719. [PMID: 20534592]

3. Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301-43312. [PMID: 22025614]

[EC 4.1.1.96 created 2012]

EC 4.1.1.97

Accepted name: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Reaction: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2

For diagram of reaction click here.

Glossary: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline

Other name(s): OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name)

Systematic name: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate carboxy-lyase [(S)-allantoin-forming]

Comments: This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans).

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

References:

1. Ramazzina, I., Folli, C., Secchi, A., Berni, R. and Percudani, R. Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat. Chem. Biol. 2 (2006) 144-148. [PMID: 16462750]

2. Cendron, L., Berni, R., Folli, C., Ramazzina, I., Percudani, R. and Zanotti, G. The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation. J. Biol. Chem. 282 (2007) 18182-18189. [PMID: 17428786]

3. Kim, K., Park, J. and Rhee, S. Structural and functional basis for (S)-allantoin formation in the ureide pathway. J. Biol. Chem. 282 (2007) 23457-23464. [PMID: 17567580]

4. French, J.B. and Ealick, S.E. Structural and mechanistic studies on Klebsiella pneumoniae 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase. J. Biol. Chem. 285 (2010) 35446-35454. [PMID: 20826786]

[EC 4.1.1.97 created 2014]

EC 4.1.1.98

Accepted name: 4-hydroxy-3-polyprenylbenzoate decarboxylase

Reaction: a 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO2

For diagram of reaction click here.

Other name(s): ubiD (gene name); 4-hydroxy-3-solanesylbenzoate decarboxylase; 3-octaprenyl-4-hydroxybenzoate decarboxylase

Systematic name: 4-hydroxy-3-polyprenylbenzoate carboxy-lyase

Comments: The enzyme catalyses a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.

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

References:

1. Leppik, R.A., Young, I.G. and Gibson, F. Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Biochim. Biophys. Acta 436 (1976) 800-810. [PMID: 782527]

2. Gulmezian, M., Hyman, K.R., Marbois, B.N., Clarke, C.F. and Javor, G.T. The role of UbiX in Escherichia coli coenzyme Q biosynthesis. Arch. Biochem. Biophys. 467 (2007) 144-153. [PMID: 17889824]

3. Pfaff, C., Glindemann, N., Gruber, J., Frentzen, M. and Sadre, R. Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase are required for plastoquinone biosynthesis in the cyanobacterium Synechocystis sp. PCC6803. J. Biol. Chem. 289 (2014) 2675-2686. [PMID: 24337576]

4. Lin, F., Ferguson, K.L., Boyer, D.R., Lin, X.N. and Marsh, E.N. Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase. ACS Chem. Biol. 10 (2015) 1137-1144. [PMID: 25647642]

5. Payne, K.A., White, M.D., Fisher, K., Khara, B., Bailey, S.S., Parker, D., Rattray, N.J., Trivedi, D.K., Goodacre, R., Beveridge, R., Barran, P., Rigby, S.E., Scrutton, N.S., Hay, S. and Leys, D. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature 522 (2015) 497-501. [PMID: 26083754]

[EC 4.1.1.98 created 2014, modified 2015]

EC 4.1.1.99

Accepted name: phosphomevalonate decarboxylase

Reaction: ATP + (R)-5-phosphomevalonate = ADP + phosphate + isopentenyl phosphate + CO2

For diagram of reaction click here

Systematic name: ATP:(R)-5-phosphomevalonate carboxy-lyase (adding ATP; isopentenyl-phosphate-forming)

Comments: The enzyme participates in a mevalonate pathway that occurs in archaea other than the extreme acidophiles of the Thermoplasmatales order. cf. EC 4.1.1.110, bisphosphomevalonate decarboxylase

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

References:

1. Vannice, J.C., Skaff, D.A., Keightley, A., Addo, J.K., Wyckoff, G.J. and Miziorko, H.M. Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway. J. Bacteriol. 196 (2014) 1055-1063. [PMID: 24375100]

[EC 4.1.1.99 created 2014, modified 2018]

EC 4.1.1.100

Accepted name: prephenate decarboxylase

Reaction: prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2

For diagram of reaction click here.

Glossary: L-anticapsin = 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine

Other name(s): BacA; AerD; SalX; non-aromatizing prephenate decarboxylase

Systematic name: prephenate carboxy-lyase (3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming)

Comments: The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme isomerizes only the pro-R double bond in prephenate.

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

References:

1. Mahlstedt, S.A. and Walsh, C.T. Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis. Biochemistry 49 (2010) 912-923. [PMID: 20052993]

2. Mahlstedt, S., Fielding, E.N., Moore, B.S. and Walsh, C.T. Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites. Biochemistry 49 (2010) 9021-9023. [PMID: 20863139]

3. Parker, J.B. and Walsh, C.T. Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis. Biochemistry 51 (2012) 3241-3251. [PMID: 22483065]

[EC 4.1.1.100 created 2015]

EC 4.1.1.101

Accepted name: malolactic enzyme

Reaction: (S)-malate = (S)-lactate + CO2

Other name(s): mleA (gene name); mleS (gene name)

Systematic name: (S)-malate carboxy-lyase

Comments: The enzyme is involved in the malolactic fermentation of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. It has been purified from several lactic acid bacteria, including Leuconostoc mesenteroides [1], Lactobacillus plantarum [2], and Oenococcus oeni [3,4]. The enzyme contains a tightly bound NAD+ cofactor and requires Mn2+.

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

References:

1. Lonvaud-Funel, A. and de Saad, A.M. Purification and properties of a malolactic Enzyme from a strain of Leuconostoc mesenteroides isolated from grapes. Appl. Environ. Microbiol. 43 (1982) 357-361. [PMID: 16345941]

2. Caspritz, G. and Radler, F. Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria. J. Biol. Chem. 258 (1983) 4907-4910. [PMID: 6833282]

3. Naouri, P., Chagnaud, P., Arnaud, A. and Galzy, P. Purification and properties of a malolactic enzyme from Leuconostoc oenos ATCC 23278. J. Basic Microbiol. 30 (1990) 577-585. [PMID: 2097345]

4. Schumann, C., Michlmayr, H., Del Hierro, A.M., Kulbe, K.D., Jiranek, V., Eder, R. and Nguyen, T.H. Malolactic enzyme from Oenococcus oeni: heterologous expression in Escherichia coli and biochemical characterization. Bioengineered 4 (2013) 147-152. [PMID: 23196745]

[EC 4.1.1.101 created 2015]

EC 4.1.1.102

Accepted name: phenacrylate decarboxylase

Reaction: (1) 4-coumarate = 4-vinylphenol + CO2
(2) trans-cinnamate = styrene + CO2
(3) ferulate = 4-vinylguaiacol + CO2

Glossary: 4-coumarate = 3-(4-hydroxyphenyl)prop-2-enoate
trans-cinnamate = (2E)-3-phenylprop-2-enoate
ferulate = 4-hydroxy-3-methoxycinnamate

Other name(s): FDC1 (gene name); ferulic acid decarboxylase

Systematic name: 3-phenylprop-2-enoate carboxy-lyase

Comments: The enzyme, found in fungi, catalyses the decarboxylation of phenacrylic acids present in plant cell walls. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.

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

References:

1. Mukai, N., Masaki, K., Fujii, T., Kawamukai, M. and Iefuji, H. PAD1 and FDC1 are essential for the decarboxylation of phenylacrylic acids in Saccharomyces cerevisiae. J. Biosci. Bioeng. 109 (2010) 564-569. [PMID: 20471595]

2. Bhuiya, M.W., Lee, S.G., Jez, J.M. and Yu, O. Structure and mechanism of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae. Appl. Environ. Microbiol. 81 (2015) 4216-4223. [PMID: 25862228]

3. Payne, K.A., White, M.D., Fisher, K., Khara, B., Bailey, S.S., Parker, D., Rattray, N.J., Trivedi, D.K., Goodacre, R., Beveridge, R., Barran, P., Rigby, S.E., Scrutton, N.S., Hay, S. and Leys, D. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature 522 (2015) 497-501. [PMID: 26083754]

[EC 4.1.1.102 created 2015]

EC 4.1.1.103

Accepted name: γ-resorcylate decarboxylase

Reaction: 2,6-dihydroxybenzoate = 1,3-dihydroxybenzene + CO2

Glossary: 2,6-dihydroxybenzoate = γ-resorcylate
1,3-dihydroxybenzene = resorcinol

Other name(s): graF (gene name); tsdA (gene name)

Systematic name: 2,6-dihydroxybenzoate carboxy-lyase

Comments: The enzyme, characterized from several bacterial strains, is involved in the degradation of γ-resorcylate. It contains a zinc ion and a water molecule at the active site. The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction.

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

References:

1. Yoshida, M., Fukuhara, N. and Oikawa, T. Thermophilic, reversible γ-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression. J. Bacteriol. 186 (2004) 6855-6863. [PMID: 15466039]

2. Ishii, Y., Narimatsu, Y., Iwasaki, Y., Arai, N., Kino, K. and Kirimura, K. Reversible and nonoxidative γ-resorcylic acid decarboxylase: characterization and gene cloning of a novel enzyme catalyzing carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium radiobacter. Biochem. Biophys. Res. Commun. 324 (2004) 611-620. [PMID: 15474471]

3. Matsui, T., Yoshida, T., Yoshimura, T. and Nagasawa, T. Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B-2. Appl. Microbiol. Biotechnol. 73 (2006) 95-102. [PMID: 16683134]

4. Goto, M., Hayashi, H., Miyahara, I., Hirotsu, K., Yoshida, M. and Oikawa, T. Crystal structures of nonoxidative zinc-dependent 2,6-dihydroxybenzoate (γ-resorcylate) decarboxylase from Rhizobium sp. strain MTP-10005. J. Biol. Chem. 281 (2006) 34365-34373. [PMID: 16963440]

5. Kasai, D., Araki, N., Motoi, K., Yoshikawa, S., Iino, T., Imai, S., Masai, E. and Fukuda, M. γ-Resorcylate catabolic-pathway genes in the soil actinomycete Rhodococcus jostii RHA1. Appl. Environ. Microbiol. 81 (2015) 7656-7665. [PMID: 26319878]

[EC 4.1.1.103 created 2016]

EC 4.1.1.104

Accepted name: 3-dehydro-4-phosphotetronate decarboxylase

Reaction: (1) 3-dehydro-4-phospho-L-erythronate = glycerone phosphate + CO2
(2) 3-dehydro-4-phospho-D-erythronate = glycerone phosphate + CO2

For diagram of reaction click here.

Glossary: L-erythronate = (2S,3S)-2,3,4-trihydroxybutanoate
D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate

Other name(s): otnC (gene name)

Systematic name: 3-dehydro-4-phosphotetronate carboxy-lyase

Comments: The enzyme, characterized from bacteria, is involved in D-erythronate and L-threonate catabolism.

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

References:

1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]

[EC 4.1.1.104 created 2017]

EC 4.1.1.105

Accepted name: L-tryptophan decarboxylase

Reaction: L-typtophan = tryptamine + CO2

For diagram of reaction click here

Other name(s): psiD (gene name); TDC (gene name)

Systematic name: L-tryptophan carboxy-lyase

Comments: The enzyme has been characterized from bacteria, plants, and fungi. Unlike EC 4.1.1.28, aromatic-L-amino-acid decarboxylase, this enzyme is specific for L-typtophan.

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

References:

1. Noe, W., Mollenschott, C. and Berlin, J. Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures: purification, molecular and kinetic data of the homogenous protein. Plant Mol. Biol. 3 (1984) 281-288. [PMID: 24310513]

2. Buki, K.G., Vinh, D.Q. and Horvath, I. Partial purification and some properties of tryptophan decarboxylase from a Bacillus strain. Acta Microbiol Hung 32 (1985) 65-73. [PMID: 4036551]

3. Nakazawa, H., Kumagai, H. and Yamada, H. Constitutive aromatic L-amino acid decarboxylase from Micrococcus percitreus. Biochem. Biophys. Res. Commun. 61 (1974) 75-82. [PMID: 4441405]

4. Lopez-Meyer, M. and Nessler, C.L. Tryptophan decarboxylase is encoded by two autonomously regulated genes in Camptotheca acuminata which are differentially expressed during development and stress. Plant J. 11 (1997) 1167-1175. [PMID: 9225462]

5. Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352-12355. [PMID: 28763571]

[EC 4.1.1.105 created 2017]

EC 4.1.1.106

Accepted name: fatty acid photodecarboxylase

Reaction: a long-chain fatty acid + = a long-chain alkane + CO2

Other name(s): FAP (gene name)

Systematic name: fatty acid carboxy-lyase (light-dependent, alkane-forming)

Comments: This algal enzyme, characterized from the green algae Chlorella variabilis and Chlamydomonas reinhardtii, is dependent on blue light, which photooxidizes its FAD cofactor. The enzyme acts on fatty acids in the range of C12 to C22, with a higher efficiency for C16 to C17 chains, and forms an alkane product that is one carbon shorter than the substrate. The enzyme can also act on unsaturated fatty acids, forming the respective alkenes, but does not generate a new double bond.

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

References:

1. Sorigue, D., Legeret, B., Cuine, S., Blangy, S., Moulin, S., Billon, E., Richaud, P., Brugiere, S., Coute, Y., Nurizzo, D., Muller, P., Brettel, K., Pignol, D., Arnoux, P., Li-Beisson, Y., Peltier, G. and Beisson, F. An algal photoenzyme converts fatty acids to hydrocarbons. Science 357 (2017) 903-907. [PMID: 28860382]

[EC 4.1.1.106 created 2017]

EC 4.1.1.107

Accepted name: 3,4-dihydroxyphenylacetaldehyde synthase

Reaction: L-dopa + O2 + H2O = 3,4-dihydroxyphenylacetaldehyde + CO2 + NH3 + H2O2

For diagram of reaction click here

Glossary: L-dopa = 3,4-dihydroxyphenylalanine

Other name(s): DHPAA synthase

Systematic name: L-dopa carboxy-lyase (oxidative-deaminating)

Comments: A pyridoxal 5'-phosphate protein. The enzyme, isolated from the mosquito Aedes aegypti, catalyses the production of 3,4-dihydroxylphenylacetaldehyde directly from L-dopa. Dopamine is not formed as an intermediate (cf. EC 4.1.1.28, aromatic-L-amino-acid decarboxylase). The enzyme is specific for L-dopa and does not react with other aromatic amino acids with the exception of a low activity with α-methyl-L-dopa.

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

References:

1. Vavricka, C., Han, Q., Huang, Y., Erickson, S.M., Harich, K., Christensen, B.M. and Li, J. From L-dopa to dihydroxyphenylacetaldehyde: a toxic biochemical pathway plays a vital physiological function in insects. PLoS One 6 (2011) e16124. [PMID: 21283636]

[EC 4.1.1.107 created 2017]

EC 4.1.1.108

Accepted name: 4-hydroxyphenylacetaldehyde synthase

Reaction: L-tyrosine + O2 + H2O = (4-hydroxyphenyl)acetaldehyde + CO2 + NH3 + H2O2

For diagram of reaction click here

Other name(s): TYRDC-2 (gene name)

Systematic name: L-tyrosine carboxy-lyase (oxidative-deaminating)

Comments: A pyridoxal 5'-phosphate protein. The enzyme, isolated from the the plant Petroselinum crispum (parsley), catalyses the production of 4-hydroxyphenylacetaldehyde directly from L-tyrosine. Tyramine is not formed as an intermediate. The enzyme has a low activity with L-dopa (cf. EC 4.1.1.107, 3,4-dihydroxyphenylacetaldehyde synthase).

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

References:

1. Torrens-Spence, M.P., Gillaspy, G., Zhao, B., Harich, K., White, R.H. and Li, J. Biochemical evaluation of a parsley tyrosine decarboxylase results in a novel 4-hydroxyphenylacetaldehyde synthase enzyme. Biochem. Biophys. Res. Commun. 418 (2012) 211-216. [PMID: 22266321]

2. Torrens-Spence, M.P., Liu, P., Ding, H., Harich, K., Gillaspy, G. and Li, J. Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases. J. Biol. Chem. 288 (2013) 2376-2387. [PMID: 23204519]

[EC 4.1.1.108 created 2017]

EC 4.1.1.109

Accepted name: phenylacetaldehyde synthase

Reaction: L-phenylalanine + O2 + H2O = phenylacetaldehyde + CO2 + NH3 + H2O2

For diagram of reaction click here

Other name(s): PAAS (gene name)

Systematic name: L-phenylalanine carboxy-lyase (oxidative-deaminating)

Comments: A pyridoxal 5'-phosphate protein. The enzyme, isolated from the the plants Petunia hybrida and a Rosa hybrid, catalyses the production of phenylacetaldehyde directly from L-phenylalanine. The enzyme is specific for L-phenylalanine and does not accept other aromatic amino acids as substrates.

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

References:

1. Kaminaga, Y., Schnepp, J., Peel, G., Kish, C.M., Ben-Nissan, G., Weiss, D., Orlova, I., Lavie, O., Rhodes, D., Wood, K., Porterfield, D.M., Cooper, A.J., Schloss, J.V., Pichersky, E., Vainstein, A. and Dudareva, N. Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation. J. Biol. Chem. 281 (2006) 23357-23366. [PMID: 16766535]

[EC 4.1.1.109 created 2017]

EC 4.1.1.110

Accepted name: bisphosphomevalonate decarboxylase

Reaction: (R)-3,5-bisphosphomevalonate = isopentenyl phosphate + CO2 + phosphate

For diagram of reaction click here.

Other name(s): mevalonate 3,5-bisphosphate decarboxylase

Systematic name: (R)-3,5-bisphosphomevalonate carboxy-lyase (isopentenyl-phosphate-forming)

Comments: The enzyme participates in an alternative mevalonate pathway that takes place in extreme acidophiles of the Thermoplasmatales order. cf. EC 4.1.1.99, phosphomevalonate decarboxylase.

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

References:

1. Vinokur, J.M., Cummins, M.C., Korman, T.P. and Bowie, J.U. An adaptation to life in acid through a novel mevalonate pathway. Sci Rep 6 (2016) 39737. [PMID: 28004831]

[EC 4.1.1.110 created 2018]

EC 4.1.1.111

Accepted name: siroheme decarboxylase

Reaction: siroheme = 12,18-didecarboxysiroheme + 2 CO2

For diagram of reaction click here.

Other name(s): sirohaem decarboxylase; nirDLHG (gene name); ahbABC (gene name)

Systematic name: siroheme carboxy-lyase

Comments: The enzyme from archaea is involved in an alternative heme biosynthesis pathway. The enzyme from denitrifying bacteria is involved in the heme d1 biosynthesis pathway.

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

References:

1. Bali, S., Lawrence, A.D., Lobo, S.A., Saraiva, L.M., Golding, B.T., Palmer, D.J., Howard, M.J., Ferguson, S.J. and Warren, M.J. Molecular hijacking of siroheme for the synthesis of heme and d1 heme. Proc. Natl Acad. Sci. USA 108 (2011) 18260-18265. [PMID: 21969545]

2. Kuhner, M., Haufschildt, K., Neumann, A., Storbeck, S., Streif, J. and Layer, G. The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri. Archaea 2014 (2014) 327637. [PMID: 24669201]

3. Palmer, D.J., Schroeder, S., Lawrence, A.D., Deery, E., Lobo, S.A., Saraiva, L.M., McLean, K.J., Munro, A.W., Ferguson, S.J., Pickersgill, R.W., Brown, D.G. and Warren, M.J. The structure, function and properties of sirohaem decarboxylase--an enzyme with structural homology to a transcription factor family that is part of the alternative haem biosynthesis pathway. Mol. Microbiol. 93 (2014) 247-261. [PMID: 24865947]

4. Haufschildt, K., Schmelz, S., Kriegler, T.M., Neumann, A., Streif, J., Arai, H., Heinz, D.W. and Layer, G. The crystal structure of siroheme decarboxylase in complex with iron-uroporphyrin III reveals two essential histidine residues. J. Mol. Biol. 426 (2014) 3272-3286. [PMID: 25083922]

[EC 4.1.1.111 created 2018]

EC 4.1.1.112

Accepted name: oxaloacetate decarboxylase

Reaction: oxaloacetate = pyruvate + CO2

Other name(s): oxaloacetate β-decarboxylase; oxalacetic acid decarboxylase; oxalate β-decarboxylase; oxaloacetate carboxy-lyase

Systematic name: oxaloacetate carboxy-lyase (pyruvate-forming)

Comments: Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic code) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme's involvement in Na+ transport.

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

References:

1. Schmitt, A., Bottke, I. and Siebert, G. Eigenschaften einer Oxaloacetat-Decarboxylase aus Dorschmuskulatur. Hoppe-Seyler's Z. Physiol. Chem. 347 (1966) 18-34. [PMID: 5972993]

2. Herbert, D. Oxalacetic carboxylase of Micrococcus lysodeikticus. Methods Enzymol. 1 (1955) 753-757.

3. Horton, A.A. and Kornberg, H.L. Oxaloacetate 4-carboxy-lyase from Pseudomonas ovalis chester. Biochim. Biophys. Acta 89 (1964) 381-383. [PMID: 14205502]

4. Sender, P.D., Martin, M.G., Peiru, S. and Magni, C. Characterization of an oxaloacetate decarboxylase that belongs to the malic enzyme family. FEBS Lett. 570 (2004) 217-222. [PMID: 15251467]

5. Narayanan, B.C., Niu, W., Han, Y., Zou, J., Mariano, P.S., Dunaway-Mariano, D. and Herzberg, O. Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily. Biochemistry 47 (2008) 167-182. [PMID: 18081320]

[EC 4.1.1.112 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, part transferred 2018 to EC 4.1.1.112]

EC 4.1.1.113

Accepted name: trans-aconitate decarboxylase

Reaction: trans-aconitate = itaconate + CO2

Glossary: trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate
itaconate = 2-methylenesuccinate

Other name(s): TAD1 (gene name)

Systematic name: trans-aconitate carboxy-lyase (itaconate-forming)

Comments: The enzyme, characterized from the smut fungus Ustilago maydis, is involved in an alternative pathway for the biosynthesis of itaconate. cf. EC 4.1.1.6, cis-aconitate decarboxylase.

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

References:

1. Geiser, E., Przybilla, S.K., Friedrich, A., Buckel, W., Wierckx, N., Blank, L.M. and Bolker, M. Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate. Microb Biotechnol 9 (2016) 116-126. [PMID: 26639528]

[EC 4.1.1.113 created 2018]

EC 4.1.1.114

Accepted name: cis-3-alkyl-4-alkyloxetan-2-one decarboxylase

Reaction: a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2

Other name(s): oleB (gene name)

Systematic name: cis-3-alkyl-4-alkyloxetan-2-one carboxy-lyase (cis-alkene-forming)

Comments: The enzyme, found in certain bacterial species, catalyses the last step in a pathway for the production of olefins.

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

References:

1. Christenson, J.K., Richman, J.E., Jensen, M.R., Neufeld, J.Y., Wilmot, C.M. and Wackett, L.P. β-Lactone synthetase found in the olefin biosynthesis pathway. Biochemistry 56 (2017) 348-351. [PMID: 28029240]

2. Christenson, J.K., Jensen, M.R., Goblirsch, B.R., Mohamed, F., Zhang, W., Wilmot, C.M. and Wackett, L.P. Active multienzyme assemblies for long-chain olefinic hydrocarbon biosynthesis. J. Bacteriol. 199 (2017) . [PMID: 28223313]

[EC 4.1.1.114 created 2018]


Continued with EC 4.1.2
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