LYSINE(144) IS ESSENTIAL FOR THE CATALYTIC ACTIVITY OF SACCHAROMYCES-CEREVISIAE TRANSALDOLASE

被引：18

作者：

MIOSGA, T ^{[1
]}

SCHAAFFGERSTENSCHLAGER, I ^{[1
]}

FRANKEN, E ^{[1
]}

ZIMMERMANN, FK ^{[1
]}

机构：

[1] TECH HSCH DARMSTADT,INST MIKROBIOL,SCHNITTSPAHNSTR 10,D-64287 DARMSTADT,GERMANY

来源：

YEAST | 1993年 / 9卷 / 11期

关键词：

TRANSALDOLASE; SACCHAROMYCES-CEREVISIAE; IN-VITRO MUTAGENESIS;

D O I：

10.1002/yea.320091111

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：

Replacement of lysine144 by glutamine in the pentose phosphate pathway enzyme transaldolase of Saccharomyces cerevisiae is associated with the complete loss of activity indicating the essential role in catalysis. Neither histidine nor cysteine is important for catalytic activity as proposed for the Candida utilis enzyme. Also we could not find any evidence for a half-site character of the enzyme as described for transaldolase of C. utilis. Therefore, the reaction mechanisms for the two enzymes are different.

引用

页码：1241 / 1249

页数：9

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