His273 of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8 is involved in the coenzyme binding.
The coenzyme binding site of NAD(+)-dependent 3-isopropylmalate dehydrogenase from Thermus thermophilus was analyzed by chemical modification and site-directed mutagenesis, and His273 of the enzyme was identified to be involved in the coenzyme binding.
Yaoi
T
T
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
Miyazaki
K
K
Oshima
T
T
D050539:3-Isopropylmalate Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology; D001483:Base Sequence; D001665:Binding Sites; D006639:Histidine; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000378:metabolism*; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000201:enzymology*
D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D009243:NAD; D006639:Histidine; D000429:Alcohol Oxidoreductases; D050539:3-Isopropylmalate Dehydrogenase