Molecular analysis of maleate cis-trans isomerase from thermophilic bacteria

被引：18

作者：

Hatakeyama, K ^{[1
]}

Goto, M ^{[1
]}

Uchida, Y ^{[1
]}

Kobayashi, M ^{[1
]}

Terasawa, M ^{[1
]}

Yukawa, H ^{[1
]}

机构：

[1] Mitsubishi Chem Corp, Biochem Lab, Ibaraki, Osaka 3000332, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2000年 / 64卷 / 03期

关键词：

maleate cis-trans isomerase; Bacillus stearothermophilus;

D O I：

10.1271/bbb.64.569

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：

Several strains of thermophilic bacteria containing maleate cis-trans isomerase were isolated from soil samples and identified as Bacillus stearothermophilus, Bacillus circulans, Bacillus Brevis, and Deleya halophila. The maleate cis-trans isomerase was purified and characterized from one of the isolated strains, B. stearothermophilus MI-102. The purified enzyme of strain MI-102 showed higher thermal stability than the enzyme of a mesophile, Alcaligenes faecalis IFO13111. The seven maleate cis-trans isomerase genes (maiA) of thermophile were cloned and sequenced. B. stearothemophilus MI-102 MaiA has 67% amino acid identity with A. faecalis MaiA. All eight amino acid sequences of maiA gene products had significant conserved regions containing cysteine residues, which were previously Suggested to be involved in an active site of the enzyme. To probe the catalytic mechanism, three cysteine residues in the conserved regions of A. faecalis MaiA were replaced with serine by site-directed mutagenesis. The results suggest that Cys80 and Cys198 play important roles in the enzyme activity.

引用

页码：569 / 576

页数：8

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