Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

被引:2
作者
Gül-Karagüler, N [1 ]
Sessions, RB [1 ]
Holbrook, JJ [1 ]
机构
[1] Sch Med Sci Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England
关键词
lactate dehydrogenase; substrate inhibition; site-directed mutagenesis;
D O I
10.1023/A:1005687723905
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.
引用
收藏
页码:395 / 399
页数:5
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