Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria

J Biol Chem. 1988 Nov 15;263(32):16872-9.

Abstract

A transhydrogenase that catalyzes the oxoacid-dependent oxidation of specific hydroxyacids has been found in rat kidney, liver, and brain. The hydroxyacids that have been found to be substrates for this enzyme are gamma-hydroxybutyrate, D-alpha-hydroxyglutarate, and L-beta-hydroxybutyrate. The oxoacids that are the best substrates for this enzyme are alpha-ketoglutarate and succinic semialdehyde; alpha-ketoadipate and oxalacetate are also substrates. This enzyme is located in the mitochondrial fraction of the cell and is not dependent on added NAD+ or NADP+.

MeSH terms

  • 3-Hydroxybutyric Acid
  • Animals
  • Chromatography, Paper
  • Gas Chromatography-Mass Spectrometry
  • Glutarates / metabolism
  • Hydrogen-Ion Concentration
  • Hydroxybutyrates / metabolism
  • Kidney / enzymology*
  • Kidney / ultrastructure
  • Kinetics
  • Mitochondria / enzymology
  • NAD / metabolism
  • NADP / metabolism
  • Rats
  • Sodium Oxybate / metabolism
  • Time Factors
  • gamma-Aminobutyric Acid / analogs & derivatives
  • gamma-Aminobutyric Acid / metabolism

Substances

  • Glutarates
  • Hydroxybutyrates
  • NAD
  • alpha-hydroxyglutarate
  • NADP
  • gamma-Aminobutyric Acid
  • Sodium Oxybate
  • succinic semialdehyde
  • 3-Hydroxybutyric Acid