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In enzymology, a tryptophanase () is an enzyme that catalyzes the chemical reaction :L-tryptophan + H2O indole + pyruvate + NH3 Thus, the two substrates of this enzyme are L-tryptophan and H2O, whereas its 3 products are indole, pyruvate, and NH3. This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan indole-lyase (deaminating; pyruvate-forming). Other names in common use include L-tryptophanase, and L-tryptophan indole-lyase (deaminating). This enzyme participates in tryptophan metabolism and nitrogen metabolism. It has 2 cofactors: pyridoxal phosphate, and Potassium. ==Structural studies== As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「tryptophanase」の詳細全文を読む スポンサード リンク
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