Biochemistry (Moscow)

, Volume 67, Issue 10, pp 1089–1098

Pyridoxal 5"-Phosphate as a Catalytic and Conformational Cofactor of Muscle Glycogen Phosphorylase b

  • N. B. Livanova
  • N. A. Chebotareva
  • T. B. Eronina
  • B. I. Kurganov
Article

DOI: 10.1023/A:1020978825802

Cite this article as:
Livanova, N.B., Chebotareva, N.A., Eronina, T.B. et al. Biochemistry (Moscow) (2002) 67: 1089. doi:10.1023/A:1020978825802

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.

glycogen phosphorylase bmechanism of reactionpyridoxal 5"-phosphateregulationthermal inactivationquaternary structure

Copyright information

© MAIK “Nauka/Interperiodica” 2002

Authors and Affiliations

  • N. B. Livanova
    • 1
  • N. A. Chebotareva
    • 1
  • T. B. Eronina
    • 1
  • B. I. Kurganov
    • 1
  1. 1.Bach Institute of BiochemistryRussian Academy of SciencesMoscowRussia