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] |
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[EC 4.1.1.1 created 1961] |
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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. [DOI] [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. [DOI] [PMID: 11546787] |
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[EC 4.1.1.2 created 1961] |
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EC
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4.1.1.3
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Transferred entry: | oxaloacetate decarboxylase. Now recognized to be two enzymes EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 4.1.1.112 (oxaloacetate decarboxylase).
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[EC 4.1.1.3 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, deleted 2018] |
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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. [DOI] [PMID: 19458715] |
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[EC 4.1.1.4 created 1961] |
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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, PDB, 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] |
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[EC 4.1.1.5 created 1961] |
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EC |
4.1.1.6 |
Accepted name: |
cis-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; cis-aconitate carboxy-lyase; CAD1 (gene name); IRG1 (gene name) |
Systematic name: |
cis-aconitate carboxy-lyase (itaconate-forming) |
Comments: |
The enzyme has been characterized from the fungus Aspergillus terreus and from human macrophages. cf. EC 4.1.1.113, trans-aconitate decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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. |
Dwiarti, L., Yamane, K., Yamatani, H., Kahar, P. and Okabe, M. Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1. J. Biosci. Bioeng. 94 (2002) 29–33. [PMID: 16233265] |
3. |
Kanamasa, S., Dwiarti, L., Okabe, M. and Park, E.Y. Cloning and functional characterization of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus. Appl. Microbiol. Biotechnol. 80 (2008) 223–229. [PMID: 18584171] |
4. |
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. [DOI] [PMID: 23610393] |
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[EC 4.1.1.6 created 1961, modified 2018] |
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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
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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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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] |
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[EC 4.1.1.7 created 1961] |
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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] |
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[EC 4.1.1.8 created 1961] |
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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, PDB, 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. [DOI] [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. |
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[EC 4.1.1.9 created 1961, deleted 1972, reinstated 1978] |
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EC
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4.1.1.10
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Deleted entry: | aminomalonate decarboxylase. Now included with EC 4.1.1.12, aspartate 4-decarboxylase |
[EC 4.1.1.10 created 1961, deleted 1972] |
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EC |
4.1.1.11 |
Accepted name: |
aspartate 1-decarboxylase |
Reaction: |
L-aspartate = β-alanine + CO2 |
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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] |
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[EC 4.1.1.11 created 1961, deleted 1972, reinstated 1984] |
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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, PDB, 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] |
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[EC 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)] |
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EC
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4.1.1.13
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Deleted entry: | carbamoylaspartate decarboxylase |
[EC 4.1.1.13 created 1961, deleted 1972] |
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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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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. [DOI] [PMID: 13918558] |
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[EC 4.1.1.14 created 1961] |
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EC |
4.1.1.15 |
Accepted name: |
glutamate decarboxylase |
Reaction: |
L-glutamate = 4-aminobutanoate + CO2 |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA
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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] |
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[EC 4.1.1.15 created 1961] |
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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] |
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[EC 4.1.1.16 created 1961] |
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EC |
4.1.1.17 |
Accepted name: |
ornithine decarboxylase |
Reaction: |
L-ornithine = putrescine + CO2 |
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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. [DOI] [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] |
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[EC 4.1.1.17 created 1961] |
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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, PDB, 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. [DOI] [PMID: 5762458] |
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[EC 4.1.1.18 created 1961] |
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EC |
4.1.1.19 |
Accepted name: |
arginine decarboxylase |
Reaction: |
L-arginine = agmatine + CO2 |
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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. [DOI] [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] |
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[EC 4.1.1.19 created 1961] |
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EC |
4.1.1.20 |
Accepted name: |
diaminopimelate decarboxylase |
Reaction: |
meso-2,6-diaminoheptanedioate = L-lysine + CO2 |
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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. [DOI] [PMID: 14378182] |
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[EC 4.1.1.20 created 1961] |
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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 |
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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. [DOI] [PMID: 9500840] |
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[EC 4.1.1.21 created 1961, modified 2000, modified 2006] |
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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: |
The enzyme from animal tissues contains a pyridoxal 5′-phosphate cofactor. The bacterial enzyme contains a tightly-bound pyruvoyl cofactor. |
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. [DOI] [PMID: 5216347] |
|
[EC 4.1.1.22 created 1961] |
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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. [DOI] [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] |
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|
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] |
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|
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. [PMID: 18871240] |
|
[EC 4.1.1.25 created 1961] |
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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] |
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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] |
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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. [DOI] [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. [PMID: 18871240] |
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. [PMID: 14054806] |
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)] |
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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. [DOI] [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] |
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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] |
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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. [DOI] [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] |
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[EC 4.1.1.31 created 1961, modified 2011] |
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EC |
4.1.1.32 |
Accepted name: |
phosphoenolpyruvate carboxykinase (GTP) |
Reaction: |
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 |
Other name(s): |
phosphoenolpyruvate carboxylase (ambiguous); phosphopyruvate carboxylase (ambiguous); phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); PEP carboxylase (ambiguous); 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] |
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[EC 4.1.1.32 created 1961] |
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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] |
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[EC 4.1.1.33 created 1961] |
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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. |
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[EC 4.1.1.34 created 1965] |
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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. |
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[EC 4.1.1.35 created 1965] |
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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] |
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[EC 4.1.1.36 created 1965] |
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EC |
4.1.1.37 |
Accepted name: |
uroporphyrinogen decarboxylase |
Reaction: |
uroporphyrinogen III = coproporphyrinogen III + 4 CO2 |
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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. [DOI] [PMID: 4984554] |
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[EC 4.1.1.37 created 1965] |
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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, PDB, 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] |
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[EC 4.1.1.38 created 1965] |
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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. [DOI] [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] |
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[EC 4.1.1.39 created 1965, modified 2001, modified 2003] |
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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. [DOI] [PMID: 14186730] |
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[EC 4.1.1.40 created 1972] |
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EC
|
4.1.1.41
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Transferred entry: | (S)-methylmalonyl-CoA decarboxylase. Now EC 7.2.4.3, (S)-methylmalonyl-CoA decarboxylase
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[EC 4.1.1.41 created 1972, modified 1983, modified 1986, deleted 2018] |
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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] |
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[EC 4.1.1.42 created 1972] |
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EC |
4.1.1.43 |
Accepted name: |
phenylpyruvate decarboxylase |
Reaction: |
phenylpyruvate = phenylacetaldehyde + CO2 |
Glossary: |
phenylpyruvate = 3-phenyl-2-oxopropanoate |
Other name(s): |
phenylpyruvate carboxy-lyase; phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming) |
Systematic name: |
3-phenyl-2-oxopropanoate carboxy-lyase (phenylacetaldehyde-forming) |
Comments: |
The enzyme from the bacterium Azospirillum brasilense also acts on some other substrates, including (indol-3-yl)pyruvate, with much lower efficiency. However, it only possesses classical Michaelis-Menten kinetics with phenylpyruvate. Aliphatic 2-oxo acids longer that 2-oxohexanoate are not substrates. cf. EC 4.1.1.74, indolepyruvate decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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. [DOI] [PMID: 4303395] |
2. |
Spaepen, S., Versees, W., Gocke, D., Pohl, M., Steyaert, J. and Vanderleyden, J. Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense. J. Bacteriol. 189 (2007) 7626–7633. [PMID: 17766418] |
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[EC 4.1.1.43 created 1972] |
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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 |
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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, PDB, 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. |
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[EC 4.1.1.44 created 1972] |
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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 |
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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, PDB, 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] |
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[EC 4.1.1.45 created 1972] |
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EC |
4.1.1.46 |
Accepted name: |
o-pyrocatechuate decarboxylase |
Reaction: |
2,3-dihydroxybenzoate = catechol + CO2 |
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For diagram of catechol biosynthesis, click here |
Other name(s): |
2,3-dihydroxybenzoate carboxy-lyase |
Systematic name: |
2,3-dihydroxybenzoate carboxy-lyase (catechol-forming) |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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. [DOI] [PMID: 6066253] |
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[EC 4.1.1.46 created 1972] |
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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. [DOI] [PMID: 13363977] |
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[EC 4.1.1.47 created 1972] |
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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 |
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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. [DOI] [PMID: 3535653] |
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[EC 4.1.1.48 created 1972] |
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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] |
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[EC 4.1.1.49 created 1972] |
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EC |
4.1.1.50 |
Accepted name: |
adenosylmethionine decarboxylase |
Reaction: |
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2 |
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For diagram of spermidine biosynthesis, click here and for diagram of spermine biosynthesis, click here |
Glossary: |
S-adenosyl 3-(methylsulfanyl)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-(methylsulfanyl)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. [DOI] |
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[EC 4.1.1.50 created 1972] |
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