Leucine transaminase

From Wikipedia, the free encyclopedia

In enzymology, a leucine transaminase (EC 2.6.1.6) is an enzyme that catalyzes the chemical reaction

L-leucine + 2-oxoglutarate $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 2.6.1.6
BRENDA references for 2.6.1.6 (Recommended.)
PubMed references for 2.6.1.6
PubMed Central references for 2.6.1.6
Google Scholar references for 2.6.1.6
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: 276–84. PMID 4968655.
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: 622–31. PMID 974100.