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

1992-01-01
MELLATI, AA
YUCEL, M
ALTINORS, N
Gündüz, Ufuk
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.
CANCER BIOCHEMISTRY BIOPHYSICS

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Citation Formats
A. MELLATI, M. YUCEL, N. ALTINORS, and U. Gündüz, “REGULATION OF M2-TYPE PYRUVATE-KINASE FROM HUMAN MENINGIOMA BY ALLOSTERIC EFFECTORS FRUCTOSE 1,6 DIPHOSPHATE AND L-ALANINE,” CANCER BIOCHEMISTRY BIOPHYSICS, pp. 33–41, 1992, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56148.