Biology:Leucine transaminase
| leucine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.6 | ||||||||
| CAS number | 9030-37-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction
- L-leucine + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] 4-methyl-2-oxopentanoate + L-glutamate
Thus, the two substrates of this enzyme are L-leucine and 2-oxoglutarate, whereas its two products are 4-methyl-2-oxopentanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. Other names in common use include L-leucine aminotransferase, leucine 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine biosynthesis, and pantothenate and coa biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
- "Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver". Biochim. Biophys. Acta 159 (2): 276–84. 1968. doi:10.1016/0005-2744(68)90076-4. PMID 4968655.
- "Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of rat liver mitochondria". Biochim. Biophys. Acta 445 (3): 622–31. 1976. doi:10.1016/0005-2744(76)90115-7. PMID 974100.
 |  |
