Characterization of methylglyoxal synthase in Saccharomyces cerevisiae

Biochem Biophys Res Commun. 1985 Aug 30;131(1):190-8. doi: 10.1016/0006-291x(85)91788-7.

Abstract

Methylglyoxal synthase in Saccharomyces cerevisiae was purified approximately 300 folds from cell extracts with 20% of activity yield. During purification procedures, polymorphic behaviours of the enzyme were observed. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis and consisted of a single polypeptide chain of Mr = 26,000. The enzyme was most active at pH 9.5-10.5 and strictly specific to dihydroxyacetone phosphate with Km = 3 mM. Phosphoenolpyruvate, glyceraldehyde-3-phosphate, orthophosphate and thiol compounds were potent inhibitors of the enzyme.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon-Oxygen Lyases*
  • Chromatography
  • Dihydroxyacetone Phosphate
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / enzymology
  • Hydrogen-Ion Concentration
  • Lyases / antagonists & inhibitors
  • Lyases / isolation & purification
  • Lyases / metabolism*
  • Molecular Weight
  • Phosphates / pharmacology
  • Phosphoenolpyruvate / pharmacology
  • Saccharomyces cerevisiae / enzymology*
  • Substrate Specificity
  • Sulfhydryl Compounds / pharmacology

Substances

  • Phosphates
  • Sulfhydryl Compounds
  • Dihydroxyacetone Phosphate
  • Phosphoenolpyruvate
  • Lyases
  • Carbon-Oxygen Lyases
  • methylglyoxal synthase