EVIDENCE FOR INVOLVEMENT OF 2 HISTIDINE-RESIDUES IN THE REACTION OF AMPICILLIN ACYLASE

被引：4

作者：

KIM, DJ ^{[1
]}

BYUN, SM ^{[1
]}

机构：

[1] KOREA INST SCI & TECHNOL, DEPT BIOL SCI & ENGN, POB 150, SEOUL 130650, SOUTH KOREA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)90896-U

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：

The chemical modification of purified ampicillin acylase by N-bromosuccinimide and diethylpyrocarbonate resulted in time-dependent inactivation of the enzyme. Both substrates, ampicillin and 6-aminopenicillanic acid, protected the enzyme against inactivation, suggesting that the modification occurred near or at the active site. Amino acid analyses and other data indicated that two histidyl residues per subunit molecule were essential for catalytic activity. © 1990.

引用

页码：904 / 908

页数：5

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