Leucine transaminase

Leucine transaminase
Identifiers
EC no.2.6.1.6
CAS no.9030-37-9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Leucine transaminase (EC 2.6.1.6) is an enzyme characterised from rat liver that catalyzes a reversible chemical reaction to interconvert L-leucine and α-ketoglutaric acid with α-ketoisocaproic acid and L-glutamic acid:[1][2]

The enzyme is a transferase, specifically a transaminase, 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. It employs one cofactor, pyridoxal phosphate.[3]

References

  1. ↑ Aki K, Ogawa K, Ichihara A (1968). "Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver". Biochim. Biophys. Acta. 159 (2): 276–84. doi:10.1016/0005-2744(68)90076-4. PMID 4968655.
  2. ↑ Ikeda T, Konishi Y, Ichihara A (1976). "Transaminase of branched chain amino acids. XI. Leucine (methionine) transaminase of rat liver mitochondria". Biochim. Biophys. Acta. 445 (3): 622–31. doi:10.1016/0005-2744(76)90115-7. PMID 974100.
  3. ↑ Enzyme 2.6.1.6 at KEGG Pathway Database.