The Enzyme Database

Displaying entries 1-50 of 770.

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EC 4.1.1.1     
Accepted name: pyruvate decarboxylase
Reaction: a 2-oxo carboxylate = an aldehyde + CO2
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase
Systematic name: 2-oxo-acid carboxy-lyase (aldehyde-forming)
Comments: A thiamine-diphosphate protein. Also catalyses acyloin formation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-04-1
References:
1.  Singer, T.P. and Pensky, J. Isolation and properties of the α-carboxylase of wheat germ. J. Biol. Chem. 196 (1952) 375–388. [PMID: 12980978]
[EC 4.1.1.1 created 1961]
 
 
EC 4.1.1.2     
Accepted name: oxalate decarboxylase
Reaction: oxalate + H+ = formate + CO2
Other name(s): oxalate carboxy-lyase
Systematic name: oxalate carboxy-lyase (formate-forming)
Comments: The enzyme from Bacillus subtilis contains manganese and requires O2 for activity, even though there is no net redox change.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-97-9
References:
1.  Jakoby, W.B., Ohmura, E. and Hayaishi, O. Enzymatic decarboxylation of oxalic acid. J. Biol. Chem. 222 (1956) 435–446. [PMID: 13367015]
2.  Tanner, A. and Bornemann, S. Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase. J. Bacteriol. 182 (2000) 5271–5273. [PMID: 10960116]
3.  Tanner, A., Bowater, L., Fairhurst, S.A. and Bornemann, S. Oxalate decarboxylase requires manganese and dioxygen for activity: Overexpression and characterization of Bacillus subtilis YvrK and YoaN. J. Biol. Chem. 276 (2001) 43627–43634. [PMID: 11546787]
[EC 4.1.1.2 created 1961]
 
 
EC 4.1.1.3     
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: The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-98-0
References:
1.  Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353–358. [PMID: 7016536]
2.  Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435–441. [PMID: 7037395]
3.  Herbert, D. Oxalacetic carboxylase of Micrococcus lysodeikticus. Methods Enzymol. 1 (1955) 753–757.
4.  Horton, A.A. and Kornberg, H.L. Oxaloacetate 4-carboxy-lyase from Pseudomonas ovalis chester. Biochim. Biophys. Acta 89 (1964) 381–383. [PMID: 14205502]
5.  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]
[EC 4.1.1.3 created 1961, modified 1986, modified 2000]
 
 
EC 4.1.1.4     
Accepted name: acetoacetate decarboxylase
Reaction: acetoacetate + H+ = acetone + CO2
For diagram of mevalonate biosynthesis, click here
Other name(s): acetoacetic acid decarboxylase; acetoacetate carboxy-lyase
Systematic name: acetoacetate carboxy-lyase (acetone-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-03-0
References:
1.  Davies, R. Studies of the acetone-butanol fermentation. 4. Acetoacetic acid decarboxylase of Cl. acetobutylicum (BY). Biochem. J. 37 (1943) 230–238. [PMID: 16747621]
2.  Zerner, B., Coutts, S.M., Lederer, F., Waters, H.H. and Westheimer, F.H. Acetoacetate decarboxylase. Preparation of the enzyme. Biochemistry 5 (1966) 813–816. [PMID: 5911291]
3.  Ho, M.C., Menetret, J.F., Tsuruta, H. and Allen, K.N. The origin of the electrostatic perturbation in acetoacetate decarboxylase. Nature 459 (2009) 393–397. [PMID: 19458715]
[EC 4.1.1.4 created 1961]
 
 
EC 4.1.1.5     
Accepted name: acetolactate decarboxylase
Reaction: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2
For diagram of reaction, click here
Other name(s): α-acetolactate decarboxylase; (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase; (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(R)-2-acetoin-forming]; (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(3R)-3-hydroxybutan-2-one-forming]
Systematic name: (2S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(3R)-3-hydroxybutan-2-one-forming]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-02-9
References:
1.  Hill, R.K., Sawada, S. and Arfin, S.M. Stereochemistry of valine and isoleucine biosynthesis. IV. Synthesis, configuration, and enzymatic specificity of α-acetolactate and α-aceto-α-hydroxybutyrate. Bioorg. Chem. 8 (1979) 175–189.
2.  Størmer, F.C. Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. J. Biol. Chem. 242 (1967) 1756–1759. [PMID: 6024768]
[EC 4.1.1.5 created 1961]
 
 
EC 4.1.1.6     
Accepted name: aconitate decarboxylase
Reaction: cis-aconitate = itaconate + CO2
Glossary: itaconate = 2-methylenesuccinate
cis-aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate
Other name(s): cis-aconitic decarboxylase; CAD; cis-aconitate carboxy-lyase
Systematic name: cis-aconitate carboxy-lyase (itaconate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-01-8
References:
1.  Bentley, R. and Thiessen, C.P. Biosynthesis of itaconic acid in Aspergillus terreus. III. The properties and reaction mechanism of cis-aconitic acid decarboxylase. J. Biol. Chem. 226 (1957) 703–720. [PMID: 13438855]
2.  Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., Buttini, M., Linster, C.L., Medina, E., Balling, R. and Hiller, K. Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc. Natl. Acad. Sci. USA 110 (2013) 7820–7825. [PMID: 23610393]
[EC 4.1.1.6 created 1961]
 
 
EC 4.1.1.7     
Accepted name: benzoylformate decarboxylase
Reaction: phenylglyoxylate = benzaldehyde + CO2
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate
Other name(s): phenylglyoxylate decarboxylase; benzoylformate carboxy-lyase; benzoylformate carboxy-lyase (benzaldehyde-forming)
Systematic name: phenylglyoxylate carboxy-lyase (benzaldehyde-forming)
Comments: A thiamine-diphosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9025-00-7
References:
1.  Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854]
[EC 4.1.1.7 created 1961]
 
 
EC 4.1.1.8     
Accepted name: oxalyl-CoA decarboxylase
Reaction: oxalyl-CoA = formyl-CoA + CO2
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): oxalyl coenzyme A decarboxylase; oxalyl-CoA carboxy-lyase
Systematic name: oxalyl-CoA carboxy-lyase (formyl-CoA-forming)
Comments: A thiamine-diphosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-96-8
References:
1.  Quayle, J.R. Carbon assimilation by Pseudomonas oxalaticus (OX1). 7. Decarboxylation of oxalyl-coenzyme A to formyl-coenzyme A. Biochem. J. 89 (1963) 492–503. [PMID: 14101969]
[EC 4.1.1.8 created 1961]
 
 
EC 4.1.1.9     
Accepted name: malonyl-CoA decarboxylase
Reaction: malonyl-CoA = acetyl-CoA + CO2
Other name(s): malonyl coenzyme A decarboxylase; malonyl-CoA carboxy-lyase
Systematic name: malonyl-CoA carboxy-lyase (acetyl-CoA-forming)
Comments: Specific for malonyl-CoA. The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 2.8.3.3 malonate CoA-transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-99-1
References:
1.  Buckner, J.S., Kolattudy, P.E. and Poulose, A.J. Purification and properties of malonyl-coenzyme A decarboxylase, a regulatory enzyme from the uropygial gland of goose. Arch. Biochem. Biophys. 177 (1976) 539–551. [PMID: 827976]
2.  Takamura, Y. and Kitayama, Y. Purification and some properties of malonate decarboxylase from Pseudomonas ovalis: an oligomeric enzyme with bifunctional properties. Biochem. Int. 3 (1981) 483–491.
[EC 4.1.1.9 created 1961, deleted 1972, reinstated 1978]
 
 
EC 4.1.1.10     
Deleted entry: aminomalonate decarboxylase. Now included with EC 4.1.1.12, aspartate 4-decarboxylase
[EC 4.1.1.10 created 1961, deleted 1972]
 
 
EC 4.1.1.11     
Accepted name: aspartate 1-decarboxylase
Reaction: L-aspartate = β-alanine + CO2
For diagram of the early stages of CoA biosynthesis, click here
Other name(s): aspartate α-decarboxylase; L-aspartate α-decarboxylase; aspartic α-decarboxylase; L-aspartate 1-carboxy-lyase
Systematic name: L-aspartate 1-carboxy-lyase (β-alanine-forming)
Comments: The Escherichia coli enzyme contains a pyruvoyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-58-2
References:
1.  Williamson, J.M. and Brown, G.M. Purification and properties of L-aspartate-α-decarboxylase, an enzyme that catalyzes the formation of β-alanine in Escherichia coli. J. Biol. Chem. 254 (1979) 8074–8082. [PMID: 381298]
[EC 4.1.1.11 created 1961, deleted 1972, reinstated 1984]
 
 
EC 4.1.1.12     
Accepted name: aspartate 4-decarboxylase
Reaction: L-aspartate = L-alanine + CO2
Other name(s): desulfinase; aminomalonic decarboxylase; aspartate β-decarboxylase; aspartate ω-decarboxylase; aspartic ω-decarboxylase; aspartic β-decarboxylase; L-aspartate β-decarboxylase; cysteine sulfinic desulfinase; L-cysteine sulfinate acid desulfinase; L-aspartate 4-carboxy-lyase
Systematic name: L-aspartate 4-carboxy-lyase (L-alanine-forming)
Comments: A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-57-1
References:
1.  Kakimoto, T., Kato, J., Shibitani, T., Nishimura, N. and Chibata, I. Crystalline L-aspartate β-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties. J. Biol. Chem. 244 (1969) 353–358. [PMID: 5773301]
2.  Novogrodsky, A. and Meister, A. Control of aspartate β-decarboxylase activity by transamination. J. Biol. Chem. 239 (1964) 879–888. [PMID: 14154469]
3.  Palekar, A.G., Tate, S.S. and Meister, A. Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine. Biochemistry 9 (1970) 2310–2315. [PMID: 5424207]
4.  Wilson, E.M. and Kornberg, H.L. Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp. Biochem. J. 88 (1963) 578–587. [PMID: 14071532]
[EC 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)]
 
 
EC 4.1.1.13     
Deleted entry:  carbamoylaspartate decarboxylase
[EC 4.1.1.13 created 1961, deleted 1972]
 
 
EC 4.1.1.14     
Accepted name: valine decarboxylase
Reaction: L-valine = 2-methylpropanamine + CO2
Other name(s): leucine decarboxylase; L-valine carboxy-lyase
Systematic name: L-valine carboxy-lyase (2-methylpropanamine-forming)
Comments: A pyridoxal-phosphate protein. Also acts on L-leucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9031-16-7
References:
1.  Sutton, C.R. and King, H.K. Inhibition of leucine decarboxylase by thiol-binding reagents. Arch. Biochem. Biophys. 96 (1962) 360–370. [PMID: 13918558]
[EC 4.1.1.14 created 1961]
 
 
EC 4.1.1.15     
Accepted name: glutamate decarboxylase
Reaction: L-glutamate = 4-aminobutanoate + CO2
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic acid decarboxylase; L-glutamate α-decarboxylase; aspartate 1-decarboxylase; aspartic α-decarboxylase; L-aspartate-α-decarboxylase; γ-glutamate decarboxylase; L-glutamate 1-carboxy-lyase
Systematic name: L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming)
Comments: A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-58-2
References:
1.  Ambe, L. and Sohonie, K. Purification and properties of glutamate decarboxylase from the field bean (Dolichos lablab). Enzymologia 26 (1963) 98–107. [PMID: 14081858]
2.  Nakano, Y. and Kitaoka, S. L-Aspartate α-decarboxylase in a cell-free system from Escherichia coli. J. Biochem. (Tokyo) 70 (1971) 327. [PMID: 4937550]
3.  Roberts, E. and Frankel, S. Further studies of glutamic acid decarboxylase in brain. J. Biol. Chem. 190 (1951) 505–512. [PMID: 14841200]
[EC 4.1.1.15 created 1961]
 
 
EC 4.1.1.16     
Accepted name: hydroxyglutamate decarboxylase
Reaction: 3-hydroxy-L-glutamate = 4-amino-3-hydroxybutanoate + CO2
Other name(s): 3-hydroxy-L-glutamate 1-carboxy-lyase
Systematic name: 3-hydroxy-L-glutamate 1-carboxy-lyase (4-amino-3-hydroxybutanoate-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-59-3
References:
1.  Umbreit, W.W. and Heneage, P. β-Hydroxyglutamic acid decarboxylase. J. Biol. Chem. 201 (1953) 15–20. [PMID: 13044771]
[EC 4.1.1.16 created 1961]
 
 
EC 4.1.1.17     
Accepted name: ornithine decarboxylase
Reaction: L-ornithine = putrescine + CO2
For diagram of spermine biosynthesis, click here and for diagram of arginine catabolism, click here
Glossary: putrescine = butane-1,4-diamine
Other name(s): SpeC; L-ornithine carboxy-lyase
Systematic name: L-ornithine carboxy-lyase (putrescine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-60-6
References:
1.  Ono, M., Inoue, H., Suzuki, F. and Takeda, Y. Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats. Purification and some properties. Biochim. Biophys. Acta 284 (1972) 285–297. [PMID: 5073764]
2.  Taylor, E.S. and Gale, E.F. Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors. Biochem. J. 39 (1945) 52–58. [PMID: 16747854]
[EC 4.1.1.17 created 1961]
 
 
EC 4.1.1.18     
Accepted name: lysine decarboxylase
Reaction: L-lysine = cadaverine + CO2
Other name(s): L-lysine carboxy-lyase
Systematic name: L-lysine carboxy-lyase (cadaverine-forming)
Comments: A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-76-4
References:
1.  Gale, E.F. and Epps, H.M.R. Studies on bacterial amino-acid decarboxylases. 1. l(+)-lysine decarboxylase. Biochem. J. 38 (1944) 232–242. [PMID: 16747785]
2.  Soda, K. and Moriguchi, M. Crystalline lysine decarboxylase. Biochem. Biophys. Res. Commun. 34 (1969) 34–39. [PMID: 5762458]
[EC 4.1.1.18 created 1961]
 
 
EC 4.1.1.19     
Accepted name: arginine decarboxylase
Reaction: L-arginine = agmatine + CO2
For diagram of arginine catabolism, click here
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): SpeA; L-arginine carboxy-lyase
Systematic name: L-arginine carboxy-lyase (agmatine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-77-5
References:
1.  Blethen, S.L., Boeker, E.A. and Snell, E.E. Arginine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme. J. Biol. Chem. 243 (1968) 1671–1677. [PMID: 4870599]
2.  Ramakrishna, S. and Adiga, P.R. Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties. Eur. J. Biochem. 59 (1975) 377–386. [PMID: 1252]
3.  Taylor, E.S. and Gale, E.F. Studies on bacterial amino-acid decarboxylases. 6. Codecarboxylase content and action of inhibitors. Biochem. J. 39 (1945) 52–58. [PMID: 16747854]
[EC 4.1.1.19 created 1961]
 
 
EC 4.1.1.20     
Accepted name: diaminopimelate decarboxylase
Reaction: meso-2,6-diaminoheptanedioate = L-lysine + CO2
Other name(s): diaminopimelic acid decarboxylase; meso-diaminopimelate decarboxylase; DAP-decarboxylase; meso-2,6-diaminoheptanedioate carboxy-lyase
Systematic name: meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-75-3
References:
1.  Denman, R.F., Hoare, D.S. and Work, E. Diaminopimelic acid decarboxylase in pyridoxin-deficient Escherichia coli. Biochim. Biophys. Acta 16 (1955) 442–443. [PMID: 14378182]
[EC 4.1.1.20 created 1961]
 
 
EC 4.1.1.21     
Accepted name: phosphoribosylaminoimidazole carboxylase
Reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
For diagram of the late stages of purine biosynthesis, click here
Other name(s): 5-phosphoribosyl-5-aminoimidazole carboxylase; 5-amino-1-ribosylimidazole 5-phosphate carboxylase; AIR carboxylase; 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase; ADE2; class II PurE; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
Systematic name: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]
Comments: While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-04-6
References:
1.  Lukens, L.N. and Buchanan, J.M. Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5′-phosphate from 5-amino-1-ribosylimidazole 5′-phosphate and carbon dioxide. J. Biol. Chem. 234 (1959) 1799–1805. [PMID: 13672967]
2.  Firestine, S.M., Poon, S.W., Mueller, E.J., Stubbe, J. and Davisson, V.J. Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms. Biochemistry 33 (1994) 11927–11934. [PMID: 7918411]
3.  Firestine, S.M., Misialek, S., Toffaletti, D.L., Klem, T.J., Perfect, J.R. and Davisson, V.J. Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis. Arch. Biochem. Biophys. 351 (1998) 123–134. [PMID: 9500840]
[EC 4.1.1.21 created 1961, modified 2000, modified 2006]
 
 
EC 4.1.1.22     
Accepted name: histidine decarboxylase
Reaction: L-histidine = histamine + CO2
Other name(s): L-histidine decarboxylase; L-histidine carboxy-lyase
Systematic name: L-histidine carboxy-lyase (histamine-forming)
Comments: A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-61-7
References:
1.  Epps, H.M.R. Studies on bacterial amino-acid decarboxylases. 4. l(–)-Histidine decarboxylase from Cl. welchii type A. Biochem. J. 39 (1945) 42–46. [PMID: 16747851]
2.  Riley, W.O. and Snell, E.E. Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic group. Biochemistry 7 (1968) 3520–3528. [PMID: 5681461]
3.  Rosenthaler, J., Guirard, B.M., Chang, G.W. and Snell, E.E. Purification and properties of histidine decarboxylase from Lactobacillus 30a. Proc. Natl. Acad. Sci. USA 54 (1965) 152–158. [PMID: 5216347]
[EC 4.1.1.22 created 1961]
 
 
EC 4.1.1.23     
Accepted name: orotidine-5′-phosphate decarboxylase
Reaction: orotidine 5′-phosphate = UMP + CO2
For diagram of pyrimidine biosynthesis, click here
Other name(s): orotidine-5′-monophosphate decarboxylase; orotodylate decarboxylase; orotidine phosphate decarboxylase; OMP decarboxylase; orotate monophosphate decarboxylase; orotidine monophosphate decarboxylase; orotidine phosphate decarboxylase; OMP-DC; orotate decarboxylase; orotidine 5′-phosphate decarboxylase; orotidylic decarboxylase; orotidylic acid decarboxylase; orotodylate decarboxylase; ODCase; orotic decarboxylase; orotidine-5′-phosphate carboxy-lyase
Systematic name: orotidine-5′-phosphate carboxy-lyase (UMP-forming)
Comments: The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-62-8
References:
1.  Jones, M.E., Kavipurapu, P.R. and Traut, T.W. Orotate phosphoribosyltransferase: orotidylate decarboxylase (Ehrlich ascites cell). Methods Enzymol. 51 (1978) 155–167. [PMID: 692383]
2.  Lieberman, I., Kornberg, A. and Simms, E.S. Enzymatic synthesis of pyrimidine nucleotides. Orotidine-5′-phosphate and uridine-5′-phosphate. J. Biol. Chem. 215 (1955) 403–415. [PMID: 14392174]
3.  McClard, R.W., Black, M.J., Livingstone, L.R. and Jones, M.E. Isolation and initial characterization of the single polypeptide that synthesizes uridine 5′-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5′-monophosphate synthase. Biochemistry 19 (1980) 4699–4706. [PMID: 6893554]
[EC 4.1.1.23 created 1961, modified 1986]
 
 
EC 4.1.1.24     
Accepted name: aminobenzoate decarboxylase
Reaction: 4(or 2)-aminobenzoate = aniline + CO2
Systematic name: aminobenzoate carboxy-lyase (aniline-forming)
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-73-1
References:
1.  McCullough, W.G., Piligian, J.T. and Daniel, I.J. Enzymatic decarboxylation of three aminobenzoates. J. Am. Chem. Soc. 79 (1957) 628–630.
[EC 4.1.1.24 created 1961]
 
 
EC 4.1.1.25     
Accepted name: tyrosine decarboxylase
Reaction: L-tyrosine = tyramine + CO2
For diagram of methanofuran biosynthesis, click here
Other name(s): L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase
Systematic name: L-tyrosine carboxy-lyase (tyramine-forming)
Comments: A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9002-09-9
References:
1.  McGilvery, R.W. and Cohen, P.P. The decarboxylation of L-phenylalanine by Streptococcus faecalis R. J. Biol. Chem. 174 (1948) 813–816.
[EC 4.1.1.25 created 1961]
 
 
EC 4.1.1.26     
Deleted entry:  DOPA decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase
[EC 4.1.1.26 created 1961, deleted 1972]
 
 
EC 4.1.1.27     
Deleted entry:  tryptophan decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase
[EC 4.1.1.27 created 1961, deleted 1972]
 
 
EC 4.1.1.28     
Accepted name: aromatic-L-amino-acid decarboxylase
Reaction: (1) L-dopa = dopamine + CO2
(2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2
For diagram of dopa biosynthesis, click here and for diagram of indole and ipecac alkaloid biosynthesis, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
L-dopa = 3,4-dihydroxyphenylalanine
Other name(s): DOPA decarboxylase; tryptophan decarboxylase; hydroxytryptophan decarboxylase; L-DOPA decarboxylase; aromatic amino acid decarboxylase; 5-hydroxytryptophan decarboxylase; aromatic-L-amino-acid carboxy-lyase (tryptamine-forming)
Systematic name: aromatic-L-amino-acid carboxy-lyase
Comments: A pyridoxal-phosphate protein. The enzyme also acts on some other aromatic L-amino acids, including L-tryptophan, L-tyrosine and L-phenylalanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9042-64-2
References:
1.  Christenson, J.G., Dairman, W. and Udenfriend, S. On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase (immunological titration-aromatic L-amino acid decarboxylase-serotonin-dopamine-norepinephrine). Proc. Natl. Acad. Sci. USA 69 (1972) 343–347. [PMID: 4536745]
2.  Lovenberg, W., Weissbach, H. and Udenfriend, S. Aromatic L-amino acid decarboxylase. J. Biol. Chem. 237 (1962) 89–93. [PMID: 14466899]
3.  McGilvery, R.W. and Cohen, P.P. The decarboxylation of L-phenylalanine by Streptococcus faecalis R. J. Biol. Chem. 174 (1948) 813–816.
4.  Sekeris, C.E. Zur Tyrosinstoffwechsel der Insekten. XII. Reinigung, Eigenschaften und Substratspezifität der DOPA-Decarboxylase. Hoppe-Seyler's Z. Physiol. Chem. 332 (1963) 70–78.
5.  Weissbach, H., Bogdanski, D.F., Redfield, B.G. and Udenfriend, S. Studies on the effect of vitamin B6 on 5-hydroxytryptamine (serotonin) formation. J. Biol. Chem. 227 (1957) 617–624. [PMID: 13462983]
[EC 4.1.1.28 created 1961 (EC 4.1.1.26 and EC 4.1.1.27 both created 1961 and incorporated 1972)]
 
 
EC 4.1.1.29     
Accepted name: sulfinoalanine decarboxylase
Reaction: 3-sulfino-L-alanine = hypotaurine + CO2
For diagram of taurine biosynthesis, click here
Other name(s): cysteine-sulfinate decarboxylase; L-cysteinesulfinic acid decarboxylase; cysteine-sulfinate decarboxylase; CADCase/CSADCase; CSAD; cysteic decarboxylase; cysteinesulfinic acid decarboxylase; cysteinesulfinate decarboxylase; sulfoalanine decarboxylase; 3-sulfino-L-alanine carboxy-lyase
Systematic name: 3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming)
Comments: A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-10-9
References:
1.  Guion-Rain, M.C., Portemer, C. and Chatagner, F. Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties. Biochim. Biophys. Acta 384 (1975) 265–276. [PMID: 236774]
2.  Jacobsen, J.G., Thomas, L.L. and Smith, L.H., Jr. Properties and distribution of mammalian L-cysteine sulfinate carboxy-lyases. Biochim. Biophys. Acta 85 (1964) 103–116. [PMID: 14159288]
[EC 4.1.1.29 created 1961, deleted 1972, reinstated 1976, modified 1983, modified 1999]
 
 
EC 4.1.1.30     
Accepted name: pantothenoylcysteine decarboxylase
Reaction: N-[(R)-pantothenoyl]-L-cysteine = pantetheine + CO2
Other name(s): pantothenylcysteine decarboxylase; N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase
Systematic name: N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase (pantetheine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-65-1
References:
1.  Brown, G.M. Pantothenylcysteine, a precursor of pantotheine in Lactobacillus helveticus. J. Biol. Chem. 226 (1957) 651–661. [PMID: 13438850]
[EC 4.1.1.30 created 1961]
 
 
EC 4.1.1.31     
Accepted name: phosphoenolpyruvate carboxylase
Reaction: phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating)
Systematic name: phosphate:oxaloacetate carboxy-lyase (adding phosphate, phosphoenolpyruvate-forming)
Comments: This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-77-0
References:
1.  Chen, J.H. and Jones, R.F. Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reeinhardtii. Biochim. Biophys. Acta 214 (1970) 318–325. [PMID: 5501374]
2.  Mazelis, M. and Vennesland, B. Carbon dioxide fixation into oxalacetate in higher plants. Plant Physiol. 32 (1957) 591–600. [PMID: 16655053]
3.  Tovar-Mendez, A., Mujica-Jimenez, C. and Munoz-Clares, R.A. Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. Plant Physiol. 123 (2000) 149–160. [PMID: 10806233]
[EC 4.1.1.31 created 1961, modified 2011]
 
 
EC 4.1.1.32     
Accepted name: phosphoenolpyruvate carboxykinase (GTP)
Reaction: GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
Other name(s): phosphoenolpyruvate carboxylase; phosphopyruvate carboxylase; phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase; phosphoenolpyruvate carboxykinase; PEP carboxylase; GTP:oxaloacetate carboxy-lyase (transphosphorylating)
Systematic name: GTP:oxaloacetate carboxy-lyase (adding GTP; phosphoenolpyruvate-forming)
Comments: ITP can act as phosphate donor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-08-5
References:
1.  Change, H.-C. and Lane, M.D. The enzymatic carboxylation of phosphoenolpyruvate. II. Purification and properties of liver mitochondrial phosphoenolpyruvate carboxykinase. J. Biol. Chem. 241 (1966) 2413–2420. [PMID: 5911620]
2.  Kurahashi, K., Pennington, R.J. and Utter, M.J. Nucleotide specificity of oxalacetic carboxylase. J. Biol. Chem. 226 (1957) 1059–1075. [PMID: 13438893]
[EC 4.1.1.32 created 1961]
 
 
EC 4.1.1.33     
Accepted name: diphosphomevalonate decarboxylase
Reaction: ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
For diagram of terpenoid biosynthesis, click here
Other name(s): pyrophosphomevalonate decarboxylase; mevalonate-5-pyrophosphate decarboxylase; pyrophosphomevalonic acid decarboxylase; 5-pyrophosphomevalonate decarboxylase; mevalonate 5-diphosphate decarboxylase; ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating)
Systematic name: ATP:(R)-5-diphosphomevalonate carboxy-lyase (adding ATP; isopentenyl-diphosphate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-66-2
References:
1.  Bloch, K., Chaykin, S., Phillips, A.H. and de Waard, A. Mevalonic acid pyrophosphate and isopentenyl pyrophosphate. J. Biol. Chem. 234 (1959) 2595–2604. [PMID: 13801508]
[EC 4.1.1.33 created 1961]
 
 
EC 4.1.1.34     
Accepted name: dehydro-L-gulonate decarboxylase
Reaction: 3-dehydro-L-gulonate = L-xylulose + CO2
Other name(s): keto-L-gulonate decarboxylase; 3-keto-L-gulonate decarboxylase; 3-dehydro-L-gulonate carboxy-lyase
Systematic name: 3-dehydro-L-gulonate carboxy-lyase (L-xylulose-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-67-3
References:
1.  Smiley, J.D. and Ashwell, G. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 357–364.
[EC 4.1.1.34 created 1965]
 
 
EC 4.1.1.35     
Accepted name: UDP-glucuronate decarboxylase
Reaction: UDP-D-glucuronate = UDP-D-xylose + CO2
For diagram of the biosynthesis of UDP-L-arabinose, UDP-galacturonate and UDP-xylose, click here
Other name(s): uridine-diphosphoglucuronate decarboxylase; UDP-D-glucuronate carboxy-lyase
Systematic name: UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming)
Comments: Requires NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-68-4
References:
1.  Ankel, H. and Feingold, D.S. Biosynthesis of uridine diphosphate D-xylose. 1. Uridine diphosphate glucuronate carboxy-lyase of wheat germ. Biochemistry 4 (1965) 2468–2475.
[EC 4.1.1.35 created 1965]
 
 
EC 4.1.1.36     
Accepted name: phosphopantothenoylcysteine decarboxylase
Reaction: N-[(R)-4′-phosphopantothenoyl]-L-cysteine = pantotheine 4′-phosphate + CO2
For diagram of the late stages of CoA biosynthesis, click here
Other name(s): 4-phosphopantotheoylcysteine decarboxylase; 4-phosphopantothenoyl-L-cysteine decarboxylase; PPC-decarboxylase; N-[(R)-4′-phosphopantothenoyl]-L-cysteine carboxy-lyase
Systematic name: N-[(R)-4′-phosphopantothenoyl]-L-cysteine carboxy-lyase (pantotheine-4′-phosphate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-69-5
References:
1.  Brown, G.M. Requirement of cytidine triphosphate for the biosynthesis of phosphopantetheine. J. Am. Chem. Soc. 80 (1958) 3161.
2.  Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370–378. [PMID: 13630913]
[EC 4.1.1.36 created 1965]
 
 
EC 4.1.1.37     
Accepted name: uroporphyrinogen decarboxylase
Reaction: uroporphyrinogen III = coproporphyrinogen III + 4 CO2
For diagram of the later stages of porphyrin biosynthesis, click here
Other name(s): uroporphyrinogen III decarboxylase; porphyrinogen carboxy-lyase; porphyrinogen decarboxylase; uroporphyrinogen-III carboxy-lyase
Systematic name: uroporphyrinogen-III carboxy-lyase (coproporphyrinogen-III-forming)
Comments: Acts on a number of porphyrinogens.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-70-8
References:
1.  Mauzerall, D. and Granick, S. Porphyrin biosynthesis in erythrocytes. III. Uroporphyrinogen and its decarboxylase. J. Biol. Chem. 232 (1958) 1141–1162. [PMID: 13549492]
2.  Tomio, J.M., Garcia, R.C., San Martin de Viale, L.C. and Grinstein, M. Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties. Biochim. Biophys. Acta 198 (1970) 353–363. [PMID: 4984554]
[EC 4.1.1.37 created 1965]
 
 
EC 4.1.1.38     
Accepted name: phosphoenolpyruvate carboxykinase (diphosphate)
Reaction: diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
Other name(s): phosphopyruvate carboxylase (ambiguous); PEP carboxyphosphotransferase (ambiguous); PEP carboxykinase (ambiguous); phosphopyruvate carboxykinase (pyrophosphate); PEP carboxylase (ambiguous); phosphopyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvate carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase; phosphoenolpyruvic carboxylase; PEPCTrP; phosphoenolpyruvic carboxykinase (pyrophosphate); phosphoenolpyruvic carboxylase (pyrophosphate); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxyphosphotransferase (ambiguous); phosphoenolpyruvic carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxylase (pyrophosphate); phosphopyruvate carboxylase (pyrophosphate); diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)
Systematic name: diphosphate:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
Comments: Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9013-12-1
References:
1.  Lochmuller, H., Wood, H.G. and Davis, J.J. Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties. J. Biol. Chem. 241 (1966) 5678–5691. [PMID: 4288896]
[EC 4.1.1.38 created 1965]
 
 
EC 4.1.1.39     
Accepted name: ribulose-bisphosphate carboxylase
Reaction: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
For diagram of reaction, click here
Other name(s): D-ribulose 1,5-diphosphate carboxylase; D-ribulose-1,5-bisphosphate carboxylase; RuBP carboxylase; carboxydismutase; diphosphoribulose carboxylase; ribulose 1,5-bisphosphate carboxylase; ribulose 1,5-bisphosphate carboxylase/oxygenase; ribulose 1,5-diphosphate carboxylase; ribulose 1,5-diphosphate carboxylase/oxygenase; ribulose bisphosphate carboxylase/oxygenase; ribulose diphosphate carboxylase; ribulose diphosphate carboxylase/oxygenase; rubisco; 3-phospho-D-glycerate carboxy-lyase (dimerizing)
Systematic name: 3-phospho-D-glycerate carboxy-lyase (dimerizing; D-ribulose-1,5-bisphosphate-forming)
Comments: Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and 2-phosphoglycolate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-23-0
References:
1.  Bowles, G., Ogren, W.L. and Hageman, R.H. Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase. Biochem. Biophys. Res. Commun. 45 (1971) 716–722. [PMID: 4331471]
2.  Wishnick, M., Lane, M.D., Scrutton, M.C. and Mildvan, A.S. The presence of tightly bound copper in ribulose diphosphate carboxylase from spinach. J. Biol. Chem. 244 (1969) 5761–5763. [PMID: 4310607]
[EC 4.1.1.39 created 1965, modified 2001, modified 2003]
 
 
EC 4.1.1.40     
Accepted name: hydroxypyruvate decarboxylase
Reaction: hydroxypyruvate = glycolaldehyde + CO2
Other name(s): hydroxypyruvate carboxy-lyase
Systematic name: hydroxypyruvate carboxy-lyase (glycolaldehyde-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-43-3
References:
1.  Hedrick, J.L. and Sallach, H.J. The nonoxidative decarboxylation of hydroxypyruvate in mammalian systems. Arch. Biochem. Biophys. 105 (1964) 261–269. [PMID: 14186730]
[EC 4.1.1.40 created 1972]
 
 
EC 4.1.1.41     
Accepted name: (S)-methylmalonyl-CoA decarboxylase
Reaction: (S)-methylmalonyl-CoA = propanoyl-CoA + CO2
Other name(s): propionyl-CoA carboxylase (incorrect); propionyl coenzyme A carboxylase (incorrect); methylmalonyl-coenzyme A decarboxylase; (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase
Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming)
Comments: The enzyme from Veillonella alcalescens is a biotinyl-protein, requires Na+ and acts as a sodium pump.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-44-4
References:
1.  Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253–1261. [PMID: 5646172]
2.  Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584–585. [PMID: 7070502]
3.  Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645–650. [PMID: 2920730]
[EC 4.1.1.41 created 1972, modified 1983, modified 1986]
 
 
EC 4.1.1.42     
Accepted name: carnitine decarboxylase
Reaction: carnitine = 2-methylcholine + CO2
Other name(s): carnitine carboxy-lyase
Systematic name: carnitine carboxy-lyase (2-methylcholine-forming)
Comments: Requires ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-38-0
References:
1.  Khairallah, E.A. and Wolf, G. Carnitine decarboxylase. The conversion of carnitine to β-methylcholine. J. Biol. Chem. 242 (1967) 32–39. [PMID: 6016331]
[EC 4.1.1.42 created 1972]
 
 
EC 4.1.1.43     
Accepted name: phenylpyruvate decarboxylase
Reaction: phenylpyruvate = phenylacetaldehyde + CO2
Other name(s): phenylpyruvate carboxy-lyase
Systematic name: phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming)
Comments: Also acts on (indol-3-yl)pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-45-5
References:
1.  Asakawa, T., Wada, H. and Yamano, T. Enzymatic conversion of phenylpyruvate to phenylacetate. Biochim. Biophys. Acta 170 (1968) 375–391. [PMID: 4303395]
[EC 4.1.1.43 created 1972]
 
 
EC 4.1.1.44     
Accepted name: 4-carboxymuconolactone decarboxylase
Reaction: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO2
For diagram of benzoate metabolism, click here
Glossary: 4-carboxymuconolactone = 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate
Other name(s): γ-4-carboxymuconolactone decarboxylase; 4-carboxymuconolactone carboxy-lyase; 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)
Systematic name: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-46-6
References:
1.  Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J. Biol. Chem. 241 (1966) 3795–3799. [PMID: 5330966]
2.  Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529–549.
[EC 4.1.1.44 created 1972]
 
 
EC 4.1.1.45     
Accepted name: aminocarboxymuconate-semialdehyde decarboxylase
Reaction: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2
For diagram of the later stages of tryptophan catabolism, click here
Glossary: aminocarboxymuconate semialdehyde = 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
Other name(s): picolinic acid carboxylase; picolinic acid decarboxylase; α-amino-β-carboxymuconate-ε-semialdehade decarboxylase; α-amino-β-carboxymuconate-ε-semialdehyde β-decarboxylase; 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase; 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
Systematic name: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming)
Comments: Product rearranges non-enzymically to picolinate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-47-7
References:
1.  Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130]
[EC 4.1.1.45 created 1972]
 
 
EC 4.1.1.46     
Accepted name: o-pyrocatechuate decarboxylase
Reaction: 2,3-dihydroxybenzoate = catechol + CO2
Other name(s): 2,3-dihydroxybenzoate carboxy-lyase
Systematic name: 2,3-dihydroxybenzoate carboxy-lyase (catechol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37289-48-8
References:
1.  Subba Rao, P.V., Moore, K., Towers, G.H.N. O-Pyrocatechiuc acid carboxy-lyase from Aspergillus niger. Arch. Biochem. Biophys. 122 (1967) 466–473. [PMID: 6066253]
[EC 4.1.1.46 created 1972]
 
 
EC 4.1.1.47     
Accepted name: tartronate-semialdehyde synthase
Reaction: 2 glyoxylate = 2-hydroxy-3-oxopropanoate + CO2
Glossary: 2-hydroxy-3-oxopropanoate = tartronate semialdehyde
Other name(s): tartronate semialdehyde carboxylase; glyoxylate carbo-ligase; glyoxylic carbo-ligase; hydroxymalonic semialdehyde carboxylase; tartronic semialdehyde carboxylase; glyoxalate carboligase; glyoxylate carboxy-lyase (dimerizing); glyoxylate carboxy-lyase (dimerizing; tartronate-semialdehyde-forming)
Systematic name: glyoxylate carboxy-lyase (dimerizing; 2-hydroxy-3-oxopropanoate-forming)
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-24-1
References:
1.  Gupta, N.K. and Vennesland, B. Glyoxylate carboligase of Escherichia coli: a flavoprotein. J. Biol. Chem. 239 (1964) 3787–3789. [PMID: 14257608]
2.  Krakow, G. and Barkulis, S.S. Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli. Biochim. Biophys. Acta 21 (1956) 593–594. [PMID: 13363977]
[EC 4.1.1.47 created 1972]
 
 
EC 4.1.1.48     
Accepted name: indole-3-glycerol-phosphate synthase
Reaction: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
For diagram of tryptophan biosynthesis, click here
Other name(s): indoleglycerol phosphate synthetase; indoleglycerol phosphate synthase; indole-3-glycerophosphate synthase; 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase (cyclizing)
Systematic name: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing; 1-C-(indol-3-yl)glycerol-3-phosphate-forming]
Comments: In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-60-1
References:
1.  Creighton, T.E. and Yanofsky, C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J. Biol. Chem. 241 (1966) 4616–4624. [PMID: 5332729]
2.  Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [PMID: 3535653]
[EC 4.1.1.48 created 1972]
 
 
EC 4.1.1.49     
Accepted name: phosphoenolpyruvate carboxykinase (ATP)
Reaction: ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2
Other name(s): phosphopyruvate carboxylase (ATP); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphopyruvate carboxykinase (adenosine triphosphate); PEP carboxylase (ambiguous); PEP carboxykinase (ambiguous); PEPCK (ATP); PEPK; PEPCK; phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxylase (ATP); phosphopyruvate carboxykinase (ambiguous); ATP:oxaloacetate carboxy-lyase (transphosphorylating)
Systematic name: ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-94-3
References:
1.  Cannata, J.J.B. Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties. J. Biol. Chem. 245 (1970) 792–798. [PMID: 5416663]
2.  Cannata, J.J.B. and Stoppani, A.O.M. Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization. J. Biol. Chem. 238 (1963) 1196–1207. [PMID: 14018315]
3.  Cannata, J.J.B. and Stoppani, A.O.M. Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme. J. Biol. Chem. 238 (1963) 1208–1212. [PMID: 14018316]
[EC 4.1.1.49 created 1972]
 
 
EC 4.1.1.50     
Accepted name: adenosylmethionine decarboxylase
Reaction: S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
For diagram of spermidine biosynthesis, click here and for diagram of spermine biosynthesis, click here
Glossary: S-adenosyl 3-(methylthio)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium
Other name(s): S-adenosylmethionine decarboxylase; S-adenosyl-L-methionine decarboxylase; S-adenosyl-L-methionine carboxy-lyase; S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
Systematic name: S-adenosyl-L-methionine carboxy-lyase [S-adenosyl 3-(methylthio)propylamine-forming]
Comments: The Escherichia coli enzyme contains a pyruvoyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-20-8
References:
1.  Anton, D.L. and Kutny, R. Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences. J. Biol. Chem. 262 (1987) 2817–2822. [PMID: 3546296]
2.  Tabor, C.W. Adenosylmethionine decarboxylase. Methods Enzymol. 5 (1962) 756–760.
[EC 4.1.1.50 created 1972]
 
 


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