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REGULATION OF M2-TYPE PYRUVATE-KINASE FROM HUMAN MENINGIOMA BY ALLOSTERIC EFFECTORS FRUCTOSE 1,6 DIPHOSPHATE AND L-ALANINE
Date
1992-01-01
Author
MELLATI, AA
YUCEL, M
ALTINORS, N
Gündüz, Ufuk
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This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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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.
Subject Keywords
Pyruvate kinase
,
Meningioma
,
Allosteric regulation
URI
https://hdl.handle.net/11511/56148
Journal
CANCER BIOCHEMISTRY BIOPHYSICS
Collections
Graduate School of Natural and Applied Sciences, Article