Roles of Arg231 and Tyr284 of Thermus thermophilus isocitrate dehydrogenase in the coenzyme specificity.
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.
Yaoi
T
T
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
Miyazaki
K
K
Oshima
T
T
D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D007521:Isocitrate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics; D014443:Tyrosine / Q000737:chemistry
D004269:DNA, Bacterial; D009243:NAD; D014443:Tyrosine; D009249:NADP; D001120:Arginine; D007521:Isocitrate Dehydrogenase