Influence of pyruvate, threonine and phosphoethanolamine on activities of some acetaldehyde-producing enzymes

Alcohol Alcohol. 1993 Jul;28(4):437-43.

Abstract

Threonine (50 mg/100 g, i.p.) leads to increased hepatic threonine aldolase activity in rats, although endogenous ethanol concentrations remain stable. After pyruvate administration (50 mg/100 g, i.p.), endogenous blood ethanol levels are raised within 30 min, but return to normal at 60 min. The activity of threonine aldolase is decreased in the liver, whereas phosphoethanolamine lyase and pyruvate dehydrogenase activities remain unchanged. Phosphoethanolamine administration (23 mg/100 g, i.p.) did not change the endogenous ethanol concentration or pyruvate dehydrogenase, threonine aldolase and phosphoethanolamine lyase activities. Pyruvate appears to be a better precursor of acetaldehyde than threonine or phosphoethanolamine.

MeSH terms

  • Acetaldehyde / blood*
  • Alcoholic Intoxication / enzymology*
  • Animals
  • Carbon-Oxygen Lyases*
  • Ethanol / pharmacokinetics
  • Ethanolamines / blood*
  • Glycine Hydroxymethyltransferase / physiology
  • Lyases / physiology
  • Male
  • Mitochondria, Liver / enzymology
  • Pyruvate Dehydrogenase Complex / physiology
  • Pyruvates / blood*
  • Pyruvic Acid
  • Rats
  • Threonine / blood*

Substances

  • Ethanolamines
  • Pyruvate Dehydrogenase Complex
  • Pyruvates
  • Threonine
  • Ethanol
  • phosphorylethanolamine
  • Pyruvic Acid
  • Glycine Hydroxymethyltransferase
  • Lyases
  • Carbon-Oxygen Lyases
  • ethanolaminephosphate phospho-lyase
  • Acetaldehyde