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In enzymology, a L-serine ammonia-lyase () is an enzyme that catalyzes the chemical reaction :L-serine pyruvate + NH3 Hence, this enzyme has one substrate, L-serine, and two products, pyruvate and NH3. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate. ==Structural studies== As of late 2007, 4 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「L-serine ammonia-lyase」の詳細全文を読む スポンサード リンク
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