Tryptophan transaminase

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In enzymology, a tryptophan transaminase (EC 2.6.1.27) is an enzyme that catalyzes the chemical reaction

L-tryptophan + 2-oxoglutarate $\rightleftharpoons$ (indol-3-yl)pyruvate + L-glutamate

Thus, the two substrates of this enzyme are L-tryptophan and 2-oxoglutarate, whereas its two products are (indol-3-yl)pyruvate 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-tryptophan:2-oxoglutarate aminotransferase. Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.

[edit] References

IUBMB entry for 2.6.1.27
BRENDA references for 2.6.1.27 (Recommended.)
PubMed references for 2.6.1.27
PubMed Central references for 2.6.1.27
Google Scholar references for 2.6.1.27
George H, Gabay S (1968). "Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase". Biochim. Biophys. Acta. 167: 555–66. PMID 5722279.
O'Neil SR, DeMoss RD (1968). "Tryptophan transaminase from Clostridium sporogenes". Arch. Biochem. Biophys. 127: 361–9. PMID 5697992.
Tangen O, Fonnum F and Haavaldsen R (1965). "Separation and purification of aromatic amino acid transaminases from rat brain". Biochim. Biophys. Acta 96: 82–90.