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In enzymology, a mandelonitrile lyase (, ''(R)-HNL'', ''(R)-oxynitrilase'', ''(R)-hydroxynitrile lyase'') is an enzyme that catalyzes the chemical reaction :mandelonitrile hydrogen cyanide + benzaldehyde Hence, this enzyme has one substrate, mandelonitrile, and two products, hydrogen cyanide and benzaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming). Other names in common use include hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, D-oxynitrilase, D-alpha-hydroxynitrile lyase, and mandelonitrile benzaldehyde-lyase. This enzyme participates in cyanoamino acid metabolism. It has 2 cofactors: flavin, and flavoprotein. ==Structural studies== As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . 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「mandelonitrile lyase」の詳細全文を読む スポンサード リンク
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