Tryptophan transaminase (EC 2.6.1.27) is an enzyme originally characterised from rat brain that catalyzes a reversible chemical reaction that interconverts L-tryptophan and α-ketoglutaric acid with indole-3-pyruvic acid and L-glutamic acid. It has also been found in pig brain and the bacterium Clostridium sporogenes. The structure of the enzyme from Arabidopsis thaliana has been determined by X-ray crystallography.
This enzyme is a transferase, specifically a transaminase, 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 and uses pyridoxal phosphate as a cofactor.
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