参与羧肽酶Y电荷中继系统的催化组氨酸残基的鉴定。
Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y.
作者信息
Jung G, Ueno H, Hayashi R, Liao T H
机构信息
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
出版信息
Protein Sci. 1995 Nov;4(11):2433-5. doi: 10.1002/pro.5560041123.
The essential histidine residue of carboxypeptidase Y (CPY) was modified by a site-specific reagent, a chloromethylketone derivative of benzyloxycarbonyl-L-phenylalanine. The single modified histidine residue was converted to N tau-carboxy-methyl histidine (cmHis) upon performic acid oxidation. A peptide containing cmHis was isolated from the tryptic-thermolytic digest. Based on the amino acid composition and sequence analysis, the peptide is shown to be Val-Phe-Asp-Gly-Gly-cmHis-MetO2-Val-Pro, which was derived from CPY cleaved by trypsin at Arg 391 and thermolysin at Phe 401, and thus His 397 was modified. This histidine residue has been implicated previously by X-ray analysis to participate in the charge-relay system of CPY.
羧肽酶Y（CPY）的必需组氨酸残基用位点特异性试剂苄氧羰基-L-苯丙氨酸的氯甲基酮衍生物进行修饰。经过甲酸氧化后，单一修饰的组氨酸残基转化为Nτ-羧甲基组氨酸（cmHis）。从胰蛋白酶-嗜热菌蛋白酶消化产物中分离出含有cmHis的肽段。基于氨基酸组成和序列分析，该肽段显示为Val-Phe-Asp-Gly-Gly-cmHis-MetO2-Val-Pro，它源自胰蛋白酶在Arg 391处和嗜热菌蛋白酶在Phe 401处切割的CPY，因此His 397被修饰。先前通过X射线分析表明该组氨酸残基参与CPY的电荷中继系统。
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