SITE-DIRECTED MUTAGENESIS OF AMP-BINDING RESIDUES IN ADENYLATE KINASE - ALTERATION OF SUBSTRATE-SPECIFICITY

被引：20

作者：

OKAJIMA, T ^{[1
]}

TANIZAWA, K ^{[1
]}

FUKUI, T ^{[1
]}

机构：

[1] OSAKA UNIV,INST SCI & IND RES,IBARAKI,OSAKA 567,JAPAN

来源：

FEBS LETTERS | 1993年 / 334卷 / 01期

关键词：

ADENYLATE KINASE; UMP-CMP KINASE; SITE-DIRECTED MUTAGENESIS; SUBSTRATE SPECIFICITY; AMP-BINDING;

D O I：

10.1016/0014-5793(93)81687-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：

Adenylate kinase is highly specific for AMP as phosphoryl acceptor. We have found that the replacement of Thr39 by Ala in the chicken muscle enzyme, alone or together with the replacement of Leu66 by Ile, caused remarkable increases in CMP and UMP activities with a concomitant decrease in AMP activity; therefore, the resulting mutant enzymes show CMP and UMP activities/AMP activity ratios much higher than the wild-type enzyme. The mutant enzyme in which Ala is substituted for Thr39 has a V(max) value for CMP comparable to that of CMP-UMP kinase.

引用

页码：86 / 88

页数：3

共 10 条

[1] THE REFINED STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM BEEF-HEART MITOCHONDRIAL MATRIX AND ITS SUBSTRATE AMP AT 1.85 A RESOLUTION [J].