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Tryptophan transaminase : ウィキペディア英語版 | Tryptophan transaminase
In enzymology, a tryptophan transaminase () is an enzyme that catalyzes the chemical reaction :L-tryptophan + 2-oxoglutarate (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. ==References==
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