Biology:Carboxyvinyl-carboxyphosphonate phosphorylmutase
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carboxyvinyl-carboxyphosphonate phosphorylmutase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.8.23 | ||||||||
CAS number | 122799-57-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a carboxyvinyl-carboxyphosphonate phosphorylmutase (EC 2.7.8.23) is an enzyme that catalyzes the chemical reaction
- 1-carboxyvinyl carboxyphosphonate [math]\displaystyle{ \rightleftharpoons }[/math] 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Hence, this enzyme has one substrate, 1-carboxyvinyl carboxyphosphonate, and two products, 3-(hydrohydroxyphosphoryl)pyruvate and CO2.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is 1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QIW.
References
- "Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus". Eur. J. Biochem. 209 (2): 735–43. 1992. doi:10.1111/j.1432-1033.1992.tb17342.x. PMID 1330557.
- "Transcriptional regulation of bialaphos biosynthesis in Streptomyces hygroscopicus". J. Bacteriol. 169 (8): 3482–8. 1987. doi:10.1128/jb.169.8.3482-3488.1987. PMID 3611020.
Original source: https://en.wikipedia.org/wiki/Carboxyvinyl-carboxyphosphonate phosphorylmutase.
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