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.

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, vol. 13, no. 1, pp. 33–41, 1992, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56148.