Kinetic Mechanism of Allosteric Regulation of Muscle Glycogen Phosphorylase b by Adenosine 5´-Monophosphate

S. V. Klinov^* and B. I. Kurganov

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow, 117071 Russia; fax: (095) 954-2732; E-mail: klinov@inbi.ras.ru

^* To whom correspondence should be addressed.

Received March 21, 2001; Revision received April 24, 2001

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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.

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KEY WORDS: glycogen phosphorylase b, kinetic mechanism, allosteric regulation

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