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 |
4.1.1.82 |
Accepted name: |
phosphonopyruvate decarboxylase |
Reaction: |
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 |
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For diagram of phosphonate metabolism, click here |
Other name(s): |
3-phosphonopyruvate carboxy-lyase |
Systematic name: |
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming) |
Comments: |
The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly. This enzyme drives the reaction catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the thermodynamically unfavourable direction of 3-phosphonopyruvate formation [2]. It is the initial step in all of the major biosynthetic pathways of phosphonate natural products [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 151662-34-9 |
References: |
1. |
Zhang, G., Dai, J., Lu, Z. and Dunaway-Mariano, D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278 (2003) 41302–41308. [DOI] [PMID: 12904299] |
2. |
Seidel, H.M. and Knowles, J.R. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. Biochemistry 33 (1994) 5641–5646. [PMID: 8180189] |
3. |
Nakashita, H., Watanabe, K., Hara, O., Hidaka, T. and Seto, H. Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P
bond formation: discovery of phosphonopyruvate decarboxylase which
catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate. J. Antibiot. (Tokyo) 50 (1997) 212–219. [PMID: 9127192] |
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[EC 4.1.1.82 created 2005] |
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EC |
4.2.1.11 |
Accepted name: |
phosphopyruvate hydratase |
Reaction: |
2-phospho-D-glycerate = phosphoenolpyruvate + H2O |
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For diagram of the Entner-Doudoroff pathway, click here |
Other name(s): |
enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydratase; 2-phosphoglycerate dehydratase; 2-phosphoglyceric dehydratase; 2-phosphoglycerate enolase; γ-enolase; 2-phospho-D-glycerate hydro-lyase |
Systematic name: |
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming) |
Comments: |
Also acts on 3-phospho-D-erythronate. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-08-8 |
References: |
1. |
Holt, A. and Wold, F. The isolation and characterization of rabbit muscle enolase. J. Biol. Chem. 236 (1961) 3227–3231. [PMID: 13908561] |
2. |
Malmström, B.G. Enolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 471–494. |
3. |
Westhead, E.W. and McLain, G. Purification of brewers’ and bakers’ yeast enolase yielding a single active component. J. Biol. Chem. 239 (1964) 2464–2468. [PMID: 14235523] |
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[EC 4.2.1.11 created 1961] |
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EC |
4.4.1.19 |
Accepted name: |
phosphosulfolactate synthase |
Reaction: |
(2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + sulfite |
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For diagram of coenzyme M biosynthesis, click here |
Other name(s): |
(2R)-phospho-3-sulfolactate synthase; (2R)-O-phospho-3-sulfolactate sulfo-lyase |
Systematic name: |
(2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase (phosphoenolpyruvate-forming) |
Comments: |
Requires Mg2+. The enzyme from the archaeon Methanococcus jannaschii catalyses the Michael addition of sulfite to phosphoenolpyruvate. It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than hydrogensulfite. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 473575-53-0 |
References: |
1. |
Graham, D.E., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes. J. Biol. Chem. 277 (2002) 13421–13429. [DOI] [PMID: 11830598] |
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[EC 4.4.1.19 created 2003] |
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EC |
5.4.2.9 |
Accepted name: |
phosphoenolpyruvate mutase |
Reaction: |
phosphoenolpyruvate = 3-phosphonopyruvate |
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For diagram of reaction, click here |
Other name(s): |
phosphoenolpyruvate-phosphonopyruvate phosphomutase; PEP phosphomutase; phosphoenolpyruvate phosphomutase; PEPPM; PEP phosphomutase |
Systematic name: |
phosphoenolpyruvate 2,3-phosphonomutase |
Comments: |
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115756-49-5 |
References: |
1. |
Bowman, E., McQueney, M., Barry, R.J. and Dunaway-Mariano, D. Catalysis and thermodynamics of the phosphoenolpyruvate phosphonopyruvate rearrangement - entry into the phosphonate class of naturally-occurring organo-phosphorus compounds. J. Am. Chem. Soc. 110 (1988) 5575–5576. |
2. |
Hikada, T., Imai, S., Hara, O., Anzai, H., Murakami, T., Nagaoka, K. and Seto, H. Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation. J. Bacteriol. 172 (1990) 3066–3072. [DOI] [PMID: 2160937] |
3. |
Seidel, H.M., Freeman, S. and Knowles, J.R. Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature 335 (1988) 457–458. [DOI] [PMID: 3138545] |
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[EC 5.4.2.9 created 1990] |
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