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通过固态核磁共振光谱法检测羧肽酶A催化肽底物水解过程中的酸酐中间体及其机理意义。

Detection of an anhydride intermediate in the carboxypeptidase A catalyzed hydrolysis of a peptide substrate by solid state NMR spectroscopy and its mechanistic implication.

作者信息

Lee H C, Ko Y H, Baek S B, Kim D H

机构信息

Department of Chemistry, Pohang University of Science and Technology, Korea.

出版信息

Bioorg Med Chem Lett. 1998 Dec 1;8(23):3379-84. doi: 10.1016/s0960-894x(98)00624-6.

DOI:10.1016/s0960-894x(98)00624-6
PMID:9873738
Abstract

We have detected an anhydride intermediate in the CPA catalyzed proteolytic reaction of Gly-Tyr. It appears that since the zinc-bound water molecule which is believed to attack the scissile amide carbonyl carbon in the hydrolysis reaction is excluded by the N-terminal amino group of Gly-Tyr, the carboxylate of Glu-270 becomes to attack the amide bond to generate the anhydride intermediate.

摘要

我们在CPA催化的Gly-Tyr蛋白水解反应中检测到一种酸酐中间体。由于在水解反应中被认为会攻击可裂解酰胺羰基碳的锌结合水分子被Gly-Tyr的N端氨基排除,Glu-270的羧酸盐似乎会攻击酰胺键以生成酸酐中间体。

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