EVIDENCE FOR INVOLVEMENT OF ARGINYL RESIDUE AT THE CATALYTIC SITE OF PENICILLIN ACYLASE FROM ESCHERICHIA-COLI

被引：15

作者：

PRABHUNE, AA

SIVARAMAN, H

机构：

[1] Division of Biochemical Sciences National Chemical Laboratory Pune -

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 173卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)81059-9

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：

Incubation of penicillin acylase from Escherichia coli with phenylglyoxal or 2,3-butanedione results in enzyme inactivation. Both benzylpenicillin and phenylacetate protect the enzyme against the inactivation, indicating the presence of arginine at or near the catalytic site. The reactions follow pseudofirst order kinetics and the inactivation kinetics indicate the presence of a single essential arginine moiety. © 1990 Academic Press, Inc.

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页码：317 / 322

页数：6

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