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绵羊肝脏细胞质醛脱氢酶中催化必需亲核残基的鉴定

Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase.

作者信息

Kitson T M, Hill J P, Midwinter G G

机构信息

Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.

出版信息

Biochem J. 1991 Apr 1;275 ( Pt 1)(Pt 1):207-10. doi: 10.1042/bj2750207.

Abstract

Sheep liver cytoplasmic aldehyde dehydrogenase was labelled by reaction with the substrate p-nitrophenyl di[14C]methylcarbamate. After tryptic digestion and peptide fractionation the labelled residue was identified as Cys-302. This is the first unequivocal identification of the essential enzymic nucleophile in the esterase activity of aldehyde dehydrogenase. By implication, Cys-302 is probably also the residue that is acylated by aldehyde substrates and the first residue that is modified by disulfiram.

摘要

绵羊肝脏细胞质醛脱氢酶通过与底物对硝基苯基二[¹⁴C]甲基氨基甲酸酯反应进行标记。经胰蛋白酶消化和肽段分级分离后,标记的残基被鉴定为Cys-302。这是醛脱氢酶酯酶活性中必需酶亲核试剂的首次明确鉴定。由此推断,Cys-302可能也是被醛底物酰化的残基,并且是被双硫仑修饰的首个残基。

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