Enzyme Nomenclature

EC 4.1

Carbon-Carbon Lyases

Sections

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


EC 4.1.1 Carboxy-Lyases

See separate file for EC 4.1.1.51 to EC 4.1.1.104.

Contents

EC 4.1.1.1 pyruvate decarboxylase
EC 4.1.1.2 oxalate decarboxylase
EC 4.1.1.3 oxaloacetate decarboxylase
EC 4.1.1.4 acetoacetate decarboxylase
EC 4.1.1.5 acetolactate decarboxylase
EC 4.1.1.6 aconitate decarboxylase
EC 4.1.1.7 benzoylformate decarboxylase
EC 4.1.1.8 oxalyl-CoA decarboxylase
EC 4.1.1.9 malonyl-CoA decarboxylase
EC 4.1.1.10 deleted, included in EC 4.1.1.12
EC 4.1.1.11 aspartate 1-decarboxylase
EC 4.1.1.12 aspartate 4-decarboxylase
EC 4.1.1.13 deleted
EC 4.1.1.14 valine decarboxylase
EC 4.1.1.15 glutamate decarboxylase
EC 4.1.1.16 hydroxyglutamate decarboxylase
EC 4.1.1.17 ornithine decarboxylase
EC 4.1.1.18 lysine decarboxylase
EC 4.1.1.19 arginine decarboxylase
EC 4.1.1.20 diaminopimelate decarboxylase
EC 4.1.1.21 phosphoribosylaminoimidazole carboxylase
EC 4.1.1.22 histidine decarboxylase
EC 4.1.1.23 orotidine-5'-phosphate decarboxylase
EC 4.1.1.24 aminobenzoate decarboxylase
EC 4.1.1.25 tyrosine decarboxylase
EC 4.1.1.26 deleted, included in EC 4.1.1.28
EC 4.1.1.27 deleted, included in EC 4.1.1.28
EC 4.1.1.28 aromatic-L-amino-acid decarboxylase
EC 4.1.1.29 sulfoalanine decarboxylase
EC 4.1.1.30 pantothenoylcysteine decarboxylase
EC 4.1.1.31 phosphoenolpyruvate carboxylase
EC 4.1.1.32 phosphoenolpyruvate carboxykinase (GTP)
EC 4.1.1.33 diphosphomevalonate decarboxylase
EC 4.1.1.34 dehydro-L-gulonate decarboxylase
EC 4.1.1.35 UDP-glucuronate decarboxylase
EC 4.1.1.36 phosphopantothenoylcysteine decarboxylase
EC 4.1.1.37 uroporphyrinogen decarboxylase
EC 4.1.1.38 phosphoenolpyruvate carboxykinase (diphosphate)
EC 4.1.1.39 ribulose-bisphosphate carboxylase
EC 4.1.1.40 hydroxypyruvate decarboxylase
EC 4.1.1.41 methylmalonyl-CoA decarboxylase
EC 4.1.1.42 carnitine decarboxylase
EC 4.1.1.43 phenylpyruvate decarboxylase
EC 4.1.1.44 4-carboxymuconolactone decarboxylase
EC 4.1.1.45 aminocarboxymuconate-semialdehyde decarboxylase
EC 4.1.1.46 o-pyrocatechuate decarboxylase
EC 4.1.1.47 tartronate-semialdehyde synthase
EC 4.1.1.48 indole-3-glycerol-phosphate synthase
EC 4.1.1.49 phosphoenolpyruvate carboxykinase (ATP)
EC 4.1.1.50 adenosylmethionine decarboxylase

See the following file for:

EC 4.1.1.51 to EC 4.1.1.104

Entries

EC 4.1.1.1

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]

[EC 4.2.1.1 created 1961, modified 2016]

EC 4.1.1.2

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 4.1.1.2 created 1961]

EC 4.1.1.3

Accepted name: oxaloacetate decarboxylase

Reaction: oxaloacetate = pyruvate + CO2

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

Systematic name: oxaloacetate carboxy-lyase

Comments: The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9024-98-0

References:

1. Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353-358. [PMID: 7016536]

2. Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435-441. [PMID: 7037395]

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

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

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

[EC 4.1.1.3 created 1961, modified 1986, modified 2000]

EC 4.1.1.4

Accepted name: acetoacetate decarboxylase

Reaction: acetoacetate + H+ = acetone + CO2

For diagram 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]

[EC 4.1.1.4 created 1961]

EC 4.1.1.5

Accepted name: acetolactate decarboxylase

Reaction: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2

For diagram 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, CAS registry number: 9025-02-9

References:

1. Hill, R.K., Sawada, S. and Arfin, S.M. Stereochemistry of valine and isoleucine biosynthesis. IV. Synthesis, configuration, and enzymatic specificity of α-acetolactate and α-aceto-α-hydroxybutyrate. Bioorg. Chem. 8 (1979) 175-189.

2. Størmer, F.C. Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. J. Biol. Chem. 242 (1967) 1756-1759. [PMID: 6024768]

[EC 4.1.1.5 created 1961]

EC 4.1.1.6

Accepted name: aconitate decarboxylase

Reaction: cis-aconitate = itaconate + CO2

Other name(s): cis-aconitic decarboxylase; CAD; cis-aconitate carboxy-lyase

Glossary: itaconic acid = 2-methylenesuccinic acid
cis-Aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate

Systematic name: cis-aconitate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-01-8

References:

1. Bentley, R. and Thiessen, C.P. Biosynthesis of itaconic acid in Aspergillus terreus. III. The properties and reaction mechanism of cis-aconitic acid decarboxylase. J. Biol. Chem. 226 (1957) 703-720.

2. Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., Buttini, M., Linster, C.L., Medina, E., Balling, R. and Hiller, K. Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc. Natl. Acad. Sci. USA 110 (2013) 7820-7825. [PMID: 23610393]

[EC 4.1.1.6 created 1961]

EC 4.1.1.7

Accepted name: benzoylformate decarboxylase

Reaction: phenylglyoxylate = benzaldehyde + CO2

Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate

Other name(s): phenylglyoxylate decarboxylase; benzoylformate carboxy-lyase

Systematic name: phenylglyoxylate carboxy-lyase

Comments: A thiamine-diphosphate protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9025-00-7

References:

1. Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the souble enzymes. J. Bacteriol. 66 (1953) 548-553.

[EC 4.1.1.7 created 1961]

EC 4.1.1.8

Accepted name: oxalyl-CoA decarboxylase

Reaction: oxalyl-CoA = formyl-CoA + CO2

Glossary: thiamine diphosphate

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.

[EC 4.1.1.8 created 1961]

EC 4.1.1.9

Accepted name: malonyl-CoA decarboxylase

Reaction: malonyl-CoA = acetyl-CoA + CO2

Other name(s): malonyl coenzyme A decarboxylase

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 4.1.1.9 created 1961, deleted 1972, reinstated 1978]

[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)]

EC 4.1.1.11

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]

[EC 4.1.1.11 created 1961, deleted 1972, reinstated 1984]

EC 4.1.1.12

Accepted name: aspartate 4-decarboxylase

Reaction: L-aspartate = L-alanine + CO2

Other name(s): desulfinase; aminomalonic decarboxylase; aspartate β-decarboxylase; aspartate ω-decarboxylase; aspartic ω-decarboxylase; aspartic β-decarboxylase; L-aspartate β-decarboxylase; cysteine sulfinic desulfinase; L-cysteine sulfinate acid desulfinase

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 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)]

[EC 4.1.1.13 Deleted entry: carbamoylaspartate decarboxylase (EC 4.1.1.13 created 1961, deleted 1972)]

EC 4.1.1.14

Accepted name: valine decarboxylase

Reaction: L-valine = 2-methylpropanamine + CO2

Other name(s): leucine decarboxylase

Systematic name: L-valine carboxy-lyase

Comments: A pyridoxal-phosphate protein. Also acts on L-leucine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9031-16-7

References:

1. Sutton, C.R. and King, H.K. Inhibition of leucine decarboxylase by thiol-binding reagents. Arch. Biochem. Biophys. 96 (1962) 360-370.

[EC 4.1.1.14 created 1961]

EC 4.1.1.15

Accepted name: glutamate decarboxylase

Reaction: L-glutamate = 4-aminobutanoate + CO2

Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA

Other name(s): L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic acid decarboxylase; L-glutamate α-decarboxylase; aspartate 1-decarboxylase; aspartic α-decarboxylase; L-aspartate-α-decarboxylase; γ-glutamate decarboxylase

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.

[EC 4.1.1.15 created 1961]

EC 4.1.1.16

Accepted name: hydroxyglutamate decarboxylase

Reaction: 3-hydroxy-L-glutamate = 4-amino-3-hydroxybutanoate + CO2

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.

[EC 4.1.1.16 created 1961]

EC 4.1.1.17

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.

[EC 4.1.1.17 created 1961]

EC 4.1.1.18

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]

[EC 4.1.1.18 created 1961]

EC 4.1.1.19

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.

[EC 4.1.1.19 created 1961]

EC 4.1.1.20

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.

[EC 4.1.1.20 created 1961]

EC 4.1.1.21

Accepted name: phosphoribosylaminoimidazole carboxylase

Reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2

For diagram, 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]

[EC 4.1.1.21 created 1961, modified 2000, modified 2006]

EC 4.1.1.22

Accepted name: histidine decarboxylase

Reaction: L-histidine = histamine + CO2

Other name(s): L-histidine decarboxylase

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]

[EC 4.1.1.22 created 1961]

EC 4.1.1.23

Accepted name: orotidine-5'-phosphate decarboxylase

Reaction: orotidine 5'-phosphate = UMP + CO2

For diagram 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]

[EC 4.1.1.23 created 1961, modified 1986]

EC 4.1.1.24

Accepted name: aminobenzoate decarboxylase

Reaction: 4(or 2)-aminobenzoate = aniline + CO2

Systematic name: aminobenzoate carboxy-lyase

Comments: A pyridoxal-phosphate protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9024-73-1

References:

1. McCullough, W.G., Piligian, J.T. and Daniel, I.J. Enzymatic decarboxylation of three aminobenzoates. J. Am. Chem. Soc. 79 (1957) 628-630.

[EC 4.1.1.24 created 1961]

EC 4.1.1.25

Accepted name: tyrosine decarboxylase

Reaction: L-tyrosine = tyramine + CO2

For diagram of 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 4.1.1.25 created 1961]

[EC 4.1.1.26 Deleted entry: DOPA decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase (EC 4.1.1.26 created 1961, deleted 1972)]

[EC 4.1.1.27 Deleted entry: tryptophan decarboxylase. Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase (EC 4.1.1.27 created 1961, deleted 1972)]

EC 4.1.1.28

Accepted name: aromatic-L-amino-acid decarboxylase

Reaction: (1) L-dopa = dopamine + CO2
(2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2

For 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]

[EC 4.1.1.28 created 1961 (EC 4.1.1.26 and EC 4.1.1.27 both created 1961 and incorporated 1972)]

EC 4.1.1.29

Accepted name: sulfinoalanine decarboxylase

Reaction: 3-sulfino-L-alanine = hypotaurine + CO2

For diagram 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.

[EC 4.1.1.29 created 1961, deleted 1972, reinstated 1976, modified 1983, modified 1999]

EC 4.1.1.30

Accepted name: pantothenoylcysteine decarboxylase

Reaction: N-[(R)-pantothenoyl]-L-cysteine = pantetheine + CO2

Other name(s): pantothenylcysteine decarboxylase

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.

[EC 4.1.1.30 created 1961]

EC 4.1.1.31

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]

[EC 4.1.1.31 created 1961, modified 2011]

EC 4.1.1.32

Accepted name: phosphoenolpyruvate carboxykinase (GTP)

Reaction: GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2

Other name(s): phosphoenolpyruvate carboxylase; phosphopyruvate carboxylase; phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase; phosphoenolpyruvate carboxykinase; PEP carboxylase

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.

[EC 4.1.1.32 created 1961]

EC 4.1.1.33

Accepted name: diphosphomevalonate decarboxylase

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

For 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.

[EC 4.1.1.33 created 1961]

EC 4.1.1.34

Accepted name: dehydro-L-gulonate decarboxylase

Reaction: 3-dehydro-L-gulonate = L-xylulose + CO2

Other name(s): keto-L-gulonate decarboxylase; 3-keto-L-gulonate decarboxylase

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.

[EC 4.1.1.34 created 1965]

EC 4.1.1.35

Accepted name: UDP-glucuronate decarboxylase

Reaction: UDP-D-glucuronate = UDP-D-xylose + CO2

For diagram of 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.

[EC 4.1.1.35 created 1965]

EC 4.1.1.36

Accepted name: phosphopantothenoylcysteine decarboxylase

Reaction: N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2

For diagram of 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.

[EC 4.1.1.36 created 1965]

EC 4.1.1.37

Accepted name: uroporphyrinogen decarboxylase

Reaction: uroporphyrinogen III = coproporphyrinogen III + 4 CO2

For diagram of 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]

[EC 4.1.1.37 created 1965]

EC 4.1.1.38

Accepted name: phosphoenolpyruvate carboxykinase (diphosphate)

Reaction: diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2

Other name(s): phosphopyruvate carboxylase (ambiguous); PEP carboxyphosphotransferase (ambiguous); PEP carboxykinase (ambiguous); phosphopyruvate carboxykinase (pyrophosphate); PEP carboxylase (ambiguous); phosphopyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvate carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase; phosphoenolpyruvic carboxylase; PEPCTrP; phosphoenolpyruvic carboxykinase (pyrophosphate); phosphoenolpyruvic carboxylase (pyrophosphate); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxyphosphotransferase (ambiguous); phosphoenolpyruvic carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxylase (pyrophosphate); phosphopyruvate carboxylase (pyrophosphate); diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)

Systematic name: diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)

Comments: Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9013-12-1

References:

1. Lochmuller, H., Wood, H.G. and Davis, J.J. Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties. J. Biol. Chem. 241 (1966) 5678-5691. [PMID: 4288896]

[EC 4.1.1.38 created 1965]

EC 4.1.1.39

Accepted name: ribulose-bisphosphate carboxylase

Reaction: 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]

[EC 4.1.1.39 created 1965, modified 2001, modified 2003]

EC 4.1.1.40

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 4.1.1.40 created 1972]

EC 4.1.1.41

Accepted name: methylmalonyl-CoA decarboxylase

Reaction: (S)-methylmalonyl-CoA = propanoyl-CoA + CO2

Other name(s): propionyl-CoA carboxylase (incorrect); propionyl coenzyme A carboxylase (incorrect); methylmalonyl-coenzyme A decarboxylase; (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase

Systematic name: (S)-methylmalonyl-CoA carboxy-lyase

Comments: The enzyme from Veillonella alcalescens is a biotinyl-protein, requires Na+ and acts as a sodium pump.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-44-4

References:

1. Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253-1261. [PMID: 5646172]

2. Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584-585. [PMID: 7070502]

3. Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645-650. [PMID: 2920730]

[EC 4.1.1.41 created 1972, modified 1983, modified 1986]

EC 4.1.1.42

Accepted name: carnitine decarboxylase

Reaction: carnitine = 2-methylcholine + CO2

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]

[EC 4.1.1.42 created 1972]

EC 4.1.1.43

Accepted name: phenylpyruvate decarboxylase

Reaction: phenylpyruvate = phenylacetaldehyde + CO2

Systematic name: phenylpyruvate carboxy-lyase

Comments: Also acts on (indol-3-yl)pyruvate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-45-5

References:

1. Asakawa, T., Wada, H. and Yamano, T. Enzymatic conversion of phenylpyruvate to phenylacetate. Biochim. Biophys. Acta 170 (1968) 375-391. [PMID: 4303395]

[EC 4.1.1.43 created 1972]

EC 4.1.1.44

Accepted name: 4-carboxymuconolactone decarboxylase

Reaction: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO2

For diagram click here.

Glossary: 4-carboxymuconolactone = 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate

Other name(s): γ-4-carboxymuconolactone decarboxylase; 4-carboxymuconolactone carboxy-lyase; 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)

Systematic name: (R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37289-46-6

References:

1. Ornston, L.N. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway. J. Biol. Chem. 241 (1966) 3795-3799. [PMID: 5330966]

2. Ornston, L.N. Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. 17A (1970) 529-549.

[EC 4.1.1.44 created 1972]

EC 4.1.1.45

Accepted name: aminocarboxymuconate-semialdehyde decarboxylase

Reaction: 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2

For diagram of 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.

[EC 4.1.1.45 created 1972]

EC 4.1.1.46

Accepted name: o-pyrocatechuate decarboxylase

Reaction: 2,3-dihydroxybenzoate = catechol + CO2

Systematic name: 2,3-dihydroxybenzoate carboxy-lyase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37289-48-8

References:

1. Subba Rao, P.V., Moore, K., Towers, G.H.N. O-Pyrocatechiuc acid carboxy-lyase from Aspergillus niger. Arch. Biochem. Biophys. 122 (1967) 466-473. [PMID: 6066253]

[EC 4.1.1.46 created 1972]

EC 4.1.1.47

Accepted name: tartronate-semialdehyde synthase

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

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

Other name(s): tartronate semialdehyde carboxylase; glyoxylate carbo-ligase; glyoxylic carbo-ligase; hydroxymalonic semialdehyde carboxylase; tartronic semialdehyde carboxylase; glyoxalate carboligase; glyoxylate carboxy-lyase (dimerizing)

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.

[EC 4.1.1.47 created 1972]

EC 4.1.1.48

Accepted name: indole-3-glycerol-phosphate synthase

Reaction: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O

For diagram 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]

[EC 4.1.1.48 created 1972]

EC 4.1.1.49

Accepted name: phosphoenolpyruvate carboxykinase (ATP)

Reaction: ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2

Other name(s): phosphopyruvate carboxylase (ATP); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphopyruvate carboxykinase (adenosine triphosphate); PEP carboxylase (ambiguous); PEP carboxykinase (ambiguous); PEPCK (ATP); PEPK; PEPCK; phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxylase (ATP); phosphopyruvate carboxykinase (ambiguous); ATP:oxaloacetate carboxy-lyase (transphosphorylating)

Systematic name: ATP:oxaloacetate carboxy-lyase (transphosphorylating)

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.

[EC 4.1.1.49 created 1972]

EC 4.1.1.50

Accepted name: adenosylmethionine decarboxylase

Reaction: S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2

For diagram of reaction click here or click here.

Other name(s): S-adenosylmethionine decarboxylase; S-adenosyl-L-methionine decarboxylase

Systematic name: S-adenosyl-L-methionine carboxy-lyase

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.

[EC 4.1.1.50 created 1972]


Continued with EC 4.1.1.51 to EC 4.1.1.104
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