Carboxyvinyl-carboxyphosphonate phosphorylmutase

In enzymology, a carboxyvinyl-carboxyphosphonate phosphorylmutase (EC 2.7.8.23) is an enzyme that catalyzes the chemical reaction

1-carboxyvinyl carboxyphosphonate 3-(hydrohydroxyphosphoryl)pyruvate + CO2
carboxyvinyl-carboxyphosphonate phosphorylmutase
Identifiers
EC number2.7.8.23
CAS number122799-57-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

gollark: Macron is bad?
gollark: Anyway, I've already generated my entry for the next round, so get fearing.
gollark: I did. It was obviously you.
gollark: It is VERY annoying that the last one has just four (4) integers in it and not five (5).
gollark: See, if you just iterate through all possible programs in some language, and see which one first produces those outputs given those inputs, you will have a solution.

References

    • Pollack SJ, Freeman S, Pompliano DL, Knowles JR (1992). "Cloning, overexpression and mechanistic studies of carboxyphosphonoenolpyruvate mutase from Streptomyces hygroscopicus". Eur. J. Biochem. 209 (2): 735–43. doi:10.1111/j.1432-1033.1992.tb17342.x. PMID 1330557.
    • Anzai H, Murakami T, Imai S, Satoh A, Nagaoka K, Thompson CJ (1987). "Transcriptional regulation of bialaphos biosynthesis in Streptomyces hygroscopicus". J. Bacteriol. 169 (8): 3482–8. PMC 212421. PMID 3611020.


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