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

doi:10.1023/a:1020978825802

Pyridoxal 5'-phosphate as a catalytic and conformational cofactor of muscle glycogen phosphorylase B

Biochemistry (Mosc). 2002 Oct;67(10):1089-98. doi: 10.1023/a:1020978825802.

Authors

N B Livanova¹, N A Chebotareva, T B Eronina, B I Kurganov

Affiliation

¹ Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071 Russia. livanova@inbi.ras.ru

PMID: 12460107
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.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Animals
Catalysis
Enzyme Stability
Glycogen Phosphorylase, Muscle Form / chemistry
Glycogen Phosphorylase, Muscle Form / metabolism*
Molecular Structure
Muscle, Skeletal / enzymology*
Protein Conformation
Pyridoxal Phosphate / chemistry
Pyridoxal Phosphate / metabolism*

Substances

Pyridoxal Phosphate
Glycogen Phosphorylase, Muscle Form