Kinetic mechanism of allosteric regulation of muscle glycogen phosphorylase B by adenosine 5'-monophosphate.
Kinetic analysis of the glycogen chain growth reaction catalyzed by glycogen phosphorylase b from rabbit skeletal muscle has been carried out over a wide range of AMP concentration under the saturation of the enzyme by glycogen. Applicability of some variants of the kinetic model involving the interaction of AMP- and glucose 1-phosphate-binding sites in the dimeric enzyme molecule is considered. A kinetic model of the enzymatic reaction describing adequately the activation of the enzyme by AMP and inhibition at sufficiently high concentrations of AMP is proposed.
Klinov
S V
SV
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow, 117071 Russia. klinov@inbi.ras.ru
Kurganov
B I
BI
D000249:Adenosine Monophosphate / Q000378:metabolism* / Q000494:pharmacology; D000494:Allosteric Regulation / Q000502:physiology; D000818:Animals; D006003:Glycogen / Q000096:biosynthesis; D024982:Glycogen Phosphorylase, Muscle Form / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D018482:Muscle, Skeletal / Q000201:enzymology*; D011817:Rabbits; D012044:Regression Analysis; D015203:Reproducibility of Results
D000249:Adenosine Monophosphate; D006003:Glycogen; D024982:Glycogen Phosphorylase, Muscle Form