Regulation of M2-type pyruvate kinase from human meningioma by allosteric effectors fructose 1,6 diphosphate and L-alanine

Cancer Biochem Biophys. 1992 Oct;13(1):33-41.

Abstract

In the present study the mechanism of action of M2-type pyruvate kinase from human meningioma in the simultaneous presence of fructose 1,6 diphosphate and L-alanine was investigated. Purified pyruvate kinase from human meningioma was allosterically inhibited by L-alanine with respect to substrates phosphoenolpyruvate and ADP. The inhibitory effects of L-alanine was partially removed by fructose 1,6 diphosphate. The purified enzyme was slightly susceptible to ATP inhibition.

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / pharmacology
  • Alanine / pharmacology
  • Allosteric Regulation
  • Fructosediphosphates / pharmacology
  • Humans
  • Hydrolysis
  • In Vitro Techniques
  • Kinetics
  • Meningeal Neoplasms / enzymology*
  • Meningioma / enzymology*
  • Phosphoenolpyruvate / metabolism
  • Pyruvate Kinase / antagonists & inhibitors
  • Pyruvate Kinase / metabolism*

Substances

  • Fructosediphosphates
  • Adenosine Diphosphate
  • Phosphoenolpyruvate
  • Adenosine Triphosphate
  • Pyruvate Kinase
  • fructose-1,6-diphosphate
  • Alanine