Valine—pyruvate transaminase

In enzymology, a valine-pyruvate transaminase (EC 2.6.1.66) is an enzyme that catalyzes the chemical reaction

L-valine + pyruvate 3-methyl-2-oxobutanoate + L-alanine
valine-pyruvate transaminase
Identifiers
EC no.2.6.1.66
CAS no.132421-38-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are L-valine and pyruvate, whereas its two products are 3-methyl-2-oxobutanoate and L-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-valine:pyruvate aminotransferase. Other names in common use include transaminase C, valine-pyruvate aminotransferase, and alanine-oxoisovalerate aminotransferase. This enzyme participates in valine, leucine and isoleucine biosynthesis.

References

    • Falkinham JO 3rd (1979). "Identification of a mutation affecting an alanine-alpha-ketoisovalerate transaminase activity in Escherichia coli K-12". Mol. Gen. Genet. 176 (1): 147–9. doi:10.1007/BF00334306. PMID 396446.
    • RUDMAN D, MEISTER A (1953). "Transamination in Escherichia coli". J. Biol. Chem. 200 (2): 591–604. PMID 13034817.


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