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Updated: Sep 28, 2026

Spectrophotometric Methods for the Study of Eukaryotic Glycogen Metabolism
Published on: August 19, 2021
Pyridoxal 5'-phosphate as a catalytic and conformational cofactor of muscle glycogen phosphorylase B
N B Livanova1, N A Chebotareva, T B Eronina
1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071 Russia. livanova@inbi.ras.ru
Abstract:
This review summarizes data on structure of muscle glycogen phosphorylase b and the role of the cofactor pyridoxal 5'-phosphate in catalysis and stabilizing the native conformation of the enzyme. Specific attention is paid to the stabilizing role of pyridoxal 5'-phosphate upon denaturation of phosphorylase b. Stability of holoenzyme, apoenzyme, and enzyme reduced by sodium borohydride is compared.
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