Valine—pyruvate transaminase
| valine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.66 | ||||||||
| CAS no. | 132421-38-6 | ||||||||
| 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 | ||||||||
| |||||||||
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
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
[edit]- 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.
{{cite journal}}: CS1 maint: numeric names: authors list (link) - RUDMAN D, MEISTER A (1953). "Transamination in Escherichia coli". J. Biol. Chem. 200 (2): 591–604. PMID 13034817.
