* To whom correspondence should be addressed.
Received April 17, 2002; Revision received May 28, 2002
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.
KEY WORDS: glycogen phosphorylase b, mechanism of reaction, pyridoxal 5´-phosphate, regulation, thermal inactivation, quaternary structure