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
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.
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.
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]
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.
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.
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.
Accepted name: methionine decarboxylase
Reaction: L-methionine = 3-methylthiopropanamine + CO2
Other name(s): L-methionine decarboxylase
Systematic name: L-methionine carboxy-lyase
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.
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.
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.
Accepted name: stipitatonate decarboxylase
Reaction: stipitatonate = stipitatate + CO2
Systematic name: stipitatonate carboxy-lyase (decyclizing)
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.
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.
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.
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.
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.
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]
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]
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.
Accepted name: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
Reaction: 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2
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
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]
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]
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]
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.
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]
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.
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]
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]
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]
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]
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.
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]
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.
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]
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]
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]
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]
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]
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]
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]
Accepted name: biotin-independent malonate decarboxylase
Reaction: malonate + H+ = acetate + CO2
For diagram of the reactions of the multienzyme complex 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 4.1.1.89, 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, 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]
Accepted name: biotin-dependent malonate decarboxylase
Reaction: malonate + H+ = acetate + CO2
For diagram of the reactions involved in the multienzyme complex click here
Other name(s): malonate decarboxylase (with biotin); malonate decarboxylase (ambiguous)
Systematic name: malonate carboxy-lyase (biotin-dependent)
Comments: Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. The enzyme described here is a biotin-dependent, Na+-translocating enzyme that includes both soluble and membrane-bound components [6]. The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88, biotin-independent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. Both enzymes achieve this 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-bound form of the enzyme. 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. In the anaerobic bacterium Malonomonas rubra, the components of the multienzyme complex/enzymes involved in carrying out the reactions of this enzyme are as follows: MadA (EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase), MadB (EC 4.3.99.2, carboxybiotin decarboxylase), MadC/MadD (EC 2.1.3.10, malonyl-S-ACP:biotin-protein carboxyltransferase) and MadH (EC 6.2.1.35, ACP-SH:acetate ligase). Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein. The carboxy group is lost with retention of configuration [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117-123. [PMID: 1628643]
2. Hilbi, H. and Dimroth, P. Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase. Arch. Microbiol. 162 (1994) 48-56. [PMID: 18251085]
3. Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2'-(5"-phosphoribosyl)-3'-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689-4696. [PMID: 8664258]
4. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]
5. Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153-1154.
6. Kim, Y.S. Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application. J. Biochem. Mol. Biol. 35 (2002) 443-451. [PMID: 12359084]
7. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]
Accepted name: peptidyl-glutamate 4-carboxylase
Reaction: peptidyl-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = peptidyl-glutamate + CO2 + O2 + phylloquinone
For diagram of reaction click here and mechanism click here.
Other name(s): vitamin K-dependent carboxylase; γ-glutamyl carboxylase
Systematic name: peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing)
Comments: The enzyme can use various vitamin-K derivatives, including menaquinone, but does not contain iron. In the reverse direction the mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational modification 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.
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]
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]
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]
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.
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 4.1.1.41 (methylmalonyl-CoA decarboxylase).
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]
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]
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]