Discrimination of aliphatic substrates by a single amino acid substitution in Bacillus badius and Bacillus sphaericus phenylalanine dehydrogenases

Biosci Biotechnol Biochem. 2009 Mar 23;73(3):729-32. doi: 10.1271/bbb.80626. Epub 2009 Mar 7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics*
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acid Substitution*
  • Amino Acids / chemistry*
  • Amino Acids / metabolism*
  • Bacillus / enzymology*
  • Kinetics
  • Mutation
  • Substrate Specificity

Substances

  • Amino Acids
  • Alcohol Oxidoreductases
  • phenylserine dehydrogenase (NADP+)