Evidence for a nicotinamide nucleotide transhydrogenase in Klebsiella pneumoniae

Biochem Biophys Res Commun. 1994 Feb 15;198(3):928-32. doi: 10.1006/bbrc.1994.1132.


Bacterial membranes from Klebsiella pneumoniae were investigated for the presence of a nicotinamide nucleotide transhydrogenase activity. Inverted membrane vesicles derived from these cells catalyzed a reduction of NAD+ or 3-acetylpyridine-NAD+ by NADPH, which showed a maximal activity of about 260 nmoles/minute per milligram protein at pH 7-8. In the presence of a protonic uncoupler the specific activity was stimulated about two-fold in this pH range. The presence of detergents did not further increase the specific activity of enzyme. The Klebsiella pneumoniae transhydrogenase activity was sensitive to phenylarsine oxide and palmityl-Coenzyme A, both of which are agents known to inhibit the mammalian enzyme. The Ki-value for palmityl-Coenzyme A with respect to NADPH was about 1.25 microM. Antibodies raised against beef heart transhydrogenase crossreacted with a 54 kD protein in the Klebsiella pneumonia membrane.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
  • Cattle
  • Cell Membrane / enzymology
  • Coenzymes / metabolism
  • Kinetics
  • Klebsiella pneumoniae / enzymology*
  • Mitochondria, Heart / enzymology
  • NAD / analogs & derivatives
  • NAD / metabolism
  • NADP Transhydrogenases / metabolism*
  • Oxidation-Reduction
  • Submitochondrial Particles / enzymology


  • Coenzymes
  • NAD
  • Carbonyl Cyanide m-Chlorophenyl Hydrazone
  • 3-acetylpyridine adenine dinucleotide
  • NADP Transhydrogenases