Regulation of M2-type pyruvate kinase from human meningioma by allosteric effectors fructose 1,6 diphosphate and L-alanine.
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.
Biology Department, Middle East Technical University, Ankara, Turkey.
A A
AA
Mellati
M
M
Yücel
N
N
Altinörs
U
U
Gündüz
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000409:Alanine / Q000494:pharmacology; D000494:Allosteric Regulation; D005635:Fructosediphosphates / Q000494:pharmacology; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008577:Meningeal Neoplasms / Q000201:enzymology*; D008579:Meningioma / Q000201:enzymology*; D010728:Phosphoenolpyruvate / Q000378:metabolism; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005635:Fructosediphosphates; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D011770:Pyruvate Kinase; C029063:fructose-1,6-diphosphate; D000409:Alanine