Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071

Appl Environ Microbiol. 2002 Feb;68(2):947-51. doi: 10.1128/AEM.68.2.947-951.2002.

Abstract

Two forms of NAD-dependent D-mandelate dehydrogenase (D-ManDHs) were purified from Enterococcus faecalis IAM 10071. While these two enzymes consistently exhibited high activity toward large 2-ketoacid substrates that were branched at the C3 or C4 position, they gave distinctly different K(m) and V(max) values for these substrates and had distinct molecular weights by gel electrophoresis and gel filtration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Alcohol Oxidoreductases / isolation & purification*
  • Alcohol Oxidoreductases / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Enterococcus faecalis / enzymology*
  • Enterococcus faecalis / growth & development
  • Kinetics
  • Lactobacillus / enzymology
  • Lactococcus lactis / enzymology
  • Molecular Weight
  • NAD / metabolism*

Substances

  • NAD
  • Alcohol Oxidoreductases
  • D-mandelate dehydrogenase