Conversion of Lactobacillus pentosus D-lactate dehydrogenase to a D-hydroxyisocaproate dehydrogenase through a single amino acid replacement

J Bacteriol. 2003 Aug;185(16):5023-6. doi: 10.1128/jb.185.16.5023-5026.2003.

Abstract

The single amino acid replacement of Tyr52 with Leu drastically increased the activity of Lactobacillus pentosus NAD-dependent D-lactate dehydrogenase toward larger aliphatic or aromatic 2-ketoacid substrates by 3 or 4 orders of magnitude and decreased the activity toward pyruvate by about 30-fold, converting the enzyme into a highly active D-2-hydroxyisocaproate dehydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / genetics*
  • Amino Acid Substitution*
  • Binding Sites
  • Caproates / chemistry
  • Caproates / metabolism*
  • Genetic Engineering
  • L-Lactate Dehydrogenase / genetics*
  • Lactobacillus / enzymology*
  • Lactobacillus / genetics
  • Models, Molecular
  • Substrate Specificity

Substances

  • Caproates
  • isocaproic acid
  • Alcohol Oxidoreductases
  • L-Lactate Dehydrogenase
  • D-2-hydroxyacid dehydrogenase