Roles of Arg231 and Tyr284 of Thermus thermophilus isocitrate dehydrogenase in the coenzyme specificity

FEBS Letters

Yaoi, Takuro¹  Oshima, Tairo¹  Miyazaki, Kentaro¹ 

[1] Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 227, Japan

关键词: Thermophile isocitrate dehydrogenase;    Site-directed mutagenesis;    Coenzyme specificity;    Thermus thermophilus;    ICDH;    isocitrate dehydrogenase;    IPMDH;    3-isopropylmalate dehydrogenase;    LDH;    lactate dehydrogenase;   

DOI  :  10.1016/0014-5793(94)01191-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The coenzyme binding site of isocitrate dehydrogenase from Thermus thermophilus was analyzed by site-directed mutagenesis. The mutation analysis revealed that Arg²³¹ and Tyr²⁸⁴ are involved in the discrimination between NAD and NADP, suggesting that these two residues interact with 2′-phosphate group of NADP.

【 授权许可】

Unknown