EC 4.1.1 Carboxy-Lyases
EC 4.1.2 Aldehyde-Lyases
EC 4.1.3 Oxo-Acid-Lyases
EC 4.1.99 Other Carbon-Carbon Lyases
See separate file for EC 4.1.1.51 to EC 4.1.1.127.
See the following file for:
EC 4.1.1.51 to EC 4.1.1.127
Accepted name: carbonic anhydrase
Reaction: H2CO3 = CO2 + H2O
Other name(s): carbonate dehydratase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; carbonate hydro-lyase (carbon-dioxide-forming)
Systematic name: carbonic acid hydro-lyase (carbon-dioxide-forming)
Comments: The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-03-0
References:
1. Keilin, D. and Mann, T. Carbonic anhydrase. Nature 144 (1939) 442-443.
2. Kannan, K.K., Ramanadham, M. and Jones, T.A. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann. N.Y. Acad. Sci. 429 (1984) 49-60. [PMID: 6430186]
3. Murakami, H. and Sly, W.S. Purification and characterization of human salivary carbonic anhydrase. J. Biol. Chem. 262 (1987) 1382-1388. [PMID: 2433278]
4. Iverson, T.M., Alber, B.E., Kisker, C., Ferry, J.G. and Rees, D.C. A closer look at the active site of γ-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39 (2000) 9222-9231. [PMID: 10924115]
5. Smith, K.S. and Ferry, J.G. Prokaryotic carbonic anhydrases. FEMS Microbiol. Rev. 24 (2000) 335-366. [PMID: 10978542]
6. Cronk, J.D., Endrizzi, J.A., Cronk, M.R., O'neill, J.W. and Zhang, K.Y. Crystal structure of E. coli β-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. Protein Sci. 10 (2001) 911-922. [PMID: 11316870]
7. Merlin, C., Masters, M., McAteer, S. and Coulson, A. Why is carbonic anhydrase essential to Escherichia coli. J. Bacteriol. 185 (2003) 6415-6424. [PMID: 14563877]
Accepted name: oxalate decarboxylase
Reaction: oxalate + H+ = formate + CO2
Systematic name: oxalate carboxy-lyase
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 4.1.1.3 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). (EC 4.1.1.3 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, deleted 2018)]
Accepted name: acetoacetate decarboxylase
Reaction: acetoacetate + H+ = acetone + CO2
For diagram click here.
Other name(s): acetoacetic acid decarboxylase
Systematic name: acetoacetate carboxy-lyase
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.
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]
Accepted name: acetolactate decarboxylase
Reaction: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2
For diagram 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]
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]
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, ExplorEnz, IUBMB, 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. [PMID: 23610393]
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
Systematic name: phenylglyoxylate carboxy-lyase
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 souble enzymes. J. Bacteriol. 66 (1953) 548-553.
Accepted name: oxalyl-CoA decarboxylase
Reaction: oxalyl-CoA = formyl-CoA + CO2
Glossary: thiamine diphosphate
Other name(s): oxalyl coenzyme A decarboxylase
Systematic name: oxalyl-CoA carboxy-lyase
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.
Accepted name: malonyl-CoA decarboxylase
Reaction: malonyl-CoA = acetyl-CoA + CO2
Other name(s): malonyl coenzyme A decarboxylase
Systematic name: malonyl-CoA carboxy-lyase
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. [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 4.1.1.10 Deleted entry: formerly aminomalonate decarboxylase. Now included with EC 4.1.1.12 aspartate 4-decarboxylase (EC 4.1.1.10 created 1961, deleted 1972)]
Accepted name: aspartate 1-decarboxylase
Reaction: L-aspartate = β-alanine + CO2
For diagram of reaction click here.
Other name(s): aspartate α-decarboxylase; L-aspartate α-decarboxylase; aspartic α-decarboxylase
Systematic name: L-aspartate 1-carboxy-lyase
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]
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
Systematic name: L-aspartate 4-carboxy-lyase
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.
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.
[EC 4.1.1.13 Deleted entry: carbamoylaspartate decarboxylase (EC 4.1.1.13 created 1961, deleted 1972)]
Accepted name: valine decarboxylase
Reaction: L-valine = 2-methylpropanamine + CO2
Other name(s): leucine decarboxylase
Systematic name: L-valine carboxy-lyase
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.
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
Systematic name: L-glutamate 1-carboxy-lyase
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.
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.
Accepted name: hydroxyglutamate decarboxylase
Reaction: 3-hydroxy-L-glutamate = 4-amino-3-hydroxybutanoate + CO2
Systematic name: 3-hydroxy-L-glutamate 1-carboxy-lyase
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.
Accepted name: ornithine decarboxylase
Reaction: L-ornithine = putrescine + CO2
For diagram of reaction click here or click here.
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.
Accepted name: lysine decarboxylase
Reaction: L-lysine = cadaverine + CO2
Systematic name: L-lysine carboxy-lyase
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.
2. Soda, K. and Moriguchi, M. Crystalline lysine decarboxylase. Biochem. Biophys. Res. Commun. 34 (1969) 34-39. [PMID: 5762458]
Accepted name: arginine decarboxylase
Reaction: L-arginine = agmatine + CO2
For diagram click here.
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): L-arginine carboxy-lyase; SpeA
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. Argenine 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 properites. 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.
Accepted name: diaminopimelate decarboxylase
Reaction: meso-2,6-diaminoheptanedioate = L-lysine + CO2
For diagram click here.
Other name(s): diaminopimelic acid decarboxylase; meso-diaminopimelate decarboxylase; DAP-decarboxylase
Systematic name: meso-2,6-diaminoheptanedioate carboxy-lyase
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.
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, 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; 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]
Accepted name: histidine decarboxylase
Reaction: L-histidine = histamine + CO2
Other name(s): L-histidine decarboxylase
Systematic name: L-histidine carboxy-lyase
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.
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]
Accepted name: orotidine-5'-phosphate decarboxylase
Reaction: orotidine 5'-phosphate = UMP + CO2
For diagram 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
Systematic name: orotidine-5'-phosphate carboxy-lyase
Comments: The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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]
Accepted name: aminobenzoate decarboxylase
Reaction: 4(or 2)-aminobenzoate = aniline + CO2
Systematic name: aminobenzoate carboxy-lyase
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.
Accepted name: tyrosine decarboxylase
Reaction: L-tyrosine = tyramine + CO2
For diagram of reaction click here.
Other name(s): L-tyrosine decarboxylase; L-(–)-tyrosine apodecarboxylase
Systematic name: L-tyrosine carboxy-lyase
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 4.1.1.26 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)]
Accepted name: aromatic-L-amino-acid decarboxylase
Reaction: (1) L-dopa = dopamine + CO2
(2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2
For diagrams of reaction click here or here.
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
L-DOPA = 3,4-dihydroxy-L-phenylalanine
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 acts on other L-amino acids including L-tryptophan.
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]
Accepted name: sulfinoalanine decarboxylase
Reaction: 3-sulfino-L-alanine = hypotaurine + CO2
For diagram 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
Systematic name: 3-sulfino-L-alanine carboxy-lyase
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.
Accepted name: pantothenoylcysteine decarboxylase
Reaction: N-[(R)-pantothenoyl]-L-cysteine = pantetheine + CO2
Other name(s): pantothenylcysteine decarboxylase
Systematic name: N-[(R)-pantothenoyl]-L-cysteine carboxy-lyase
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.
Accepted name: phosphoenolpyruvate carboxylase
Reaction: phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-
For diagram of reaction 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, PDB, Metacyc, 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]
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 (transphosphorylating)
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.
Accepted name: diphosphomevalonate decarboxylase
Reaction: ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2
For reaction pathway click here.
Other name(s): pyrophosphomevalonate decarboxylase; mevalonate-5-pyrophosphate decarboxylase; pyrophosphomevalonic acid decarboxylase; 5-pyrophosphomevalonate decarboxylase; mevalonate 5-diphosphate decarboxylase
Systematic name: ATP:(R)-5-diphosphomevalonate carboxy-lyase (dehydrating)
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 isopentenylpyrophosphate. J. Biol. Chem. 234 (1959) 2595-2604.
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
Systematic name: 3-dehydro-L-gulonate carboxy-lyase
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-gulonic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 357-364.
Accepted name: UDP-glucuronate decarboxylase
Reaction: UDP-D-glucuronate = UDP-D-xylose + CO2
For diagram of reaction click here.
Other name(s): uridine-diphosphoglucuronate decarboxylase
Systematic name: UDP-D-glucuronate carboxy-lyase
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.
Accepted name: phosphopantothenoylcysteine decarboxylase
Reaction: N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
For diagram of reaction 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 only.
2. Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370-378.
Accepted name: uroporphyrinogen decarboxylase
Reaction: uroporphyrinogen III = coproporphyrinogen III + 4 CO2
For diagram of reaction 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.
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]
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)
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]
Accepted name: ribulose-bisphosphate carboxylase
Reaction: D-ribulose 1,5-bisphosphate + CO2 + H2O = 2 3-phospho-D-glycerate + 2 H+
For diagram 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
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]
Accepted name: hydroxypyruvate decarboxylase
Reaction: hydroxypyruvate = glycolaldehyde + CO2
Systematic name: hydroxypyruvate carboxy-lyase
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.
[EC 4.1.1.41 Transferred entry: (S)-methylmalonyl-CoA decarboxylase. Now EC 7.2.4.3, (S)-methylmalonyl-CoA decarboxylase (EC 4.1.1.41 created 1972, modified 1983, modified 1986, deleted 2018)]
Accepted name: carnitine decarboxylase
Reaction: carnitine = 2-methylcholine + CO2
Systematic name: carnitine carboxy-lyase
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]
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. [PMID: 4303395]
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 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.
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 reaction click here.
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
Systematic name: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase
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.
Accepted name: o-pyrocatechuate decarboxylase
Reaction: 2,3-dihydroxybenzoate = catechol + CO2
For diagram of reaction click here.
Systematic name: 2,3-dihydroxybenzoate carboxy-lyase
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. [PMID: 6066253]
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)
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.
2. Krakow, G. and Barkulis, S.S. Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli. Biochim. Biophys. Acta 21 (1956) 593-594.
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 click here.
Other name(s): indoleglycerol phosphate synthetase; indoleglycerol phosphate synthase; indole-3-glycerophosphate synthase
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 biosynthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55-77. [PMID: 16526091]
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)
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.
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.
Accepted name: adenosylmethionine decarboxylase
Reaction: S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
For diagram of reaction click here or click here.
Other name(s): S-adenosylmethionine decarboxylase; S-adenosyl-L-methionine decarboxylase; 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.A.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.