Discrimination of aliphatic substrates by a single amino acid substitution in Bacillus badius and Bacillus sphaericus phenylalanine dehydrogenases.
Replacement of glycine by serine at positions 123 and 124 of phenylalanine dehydrogenases from Bacillus badius and Bacillus sphaericus respectively strikingly decreased enzyme activity toward aromatic amino acids and resulted in an elevation of relative activity toward aliphatic amino acids. The mutant from B. badius preferentially dehydrogenated branched-chain amino acids, while that from B. sphaericus acted on amino acids with straight-chain amino acids.
Tachibana
Shinjiro
S
Biotechnology Research Center, Toyama Prefectural University, Imizu, Toyama, Japan.
Kuwamori
Yuko
Y
Asano
Yasuhisa
Y
D000429:Alcohol Oxidoreductases / Q000235:genetics* / Q000378:metabolism*; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D007700:Kinetics; D009154:Mutation; D013379:Substrate Specificity
D000596:Amino Acids; D000429:Alcohol Oxidoreductases; C086412:phenylserine dehydrogenase (NADP+)