REGULATION OF M2-TYPE PYRUVATE-KINASE FROM HUMAN MENINGIOMA BY ALLOSTERIC EFFECTORS FRUCTOSE 1,6 DIPHOSPHATE AND L-ALANINE


MELLATI A., YUCEL M., ALTINORS N., GUNDUZ U.

CANCER BIOCHEMISTRY BIOPHYSICS, vol.13, no.1, pp.33-41, 1992 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 13 Issue: 1
  • Publication Date: 1992
  • Title of Journal : CANCER BIOCHEMISTRY BIOPHYSICS
  • Page Numbers: pp.33-41
  • Keywords: PYRUVATE KINASE, MENINGIOMA, ALLOSTERIC REGULATION, MULTIMOLECULAR FORMS, PURIFICATION, GLIOMAS, RAT, ISOENZYMES, INHIBITION, ISOZYMES, TYPE-M1, BRAIN

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.