CHEMICAL MODIFICATION LOCATES GUANIDINYL AND CARBOXYLATE GROUPS WITHIN THE ACTIVE-SITE OF PROLIDASE

被引：10

作者：

MOCK, WL

ZHUANG, H

机构：

[1] Department of Chemistry, University of Illinois at Chicago, Chicago

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0006-291X(05)81307-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline. The presence of arginine and carboxylate (aspartic/glutamic acid) residues at the active site of this metallodipeptidase may be inferred. © 1991 Academic Press, Inc.

引用

页码：401 / 406

页数：6

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