RGD Reference Report - Structural relationships among regulated and unregulated phosphorylases. - Rat Genome Database

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Structural relationships among regulated and unregulated phosphorylases.

Authors: Buchbinder, JL  Rath, VL  Fletterick, RJ 
Citation: Buchbinder JL, etal., Annu Rev Biophys Biomol Struct. 2001;30:191-209.
RGD ID: 1642822
Pubmed: PMID:11340058   (View Abstract at PubMed)
DOI: DOI:10.1146/annurev.biophys.30.1.191   (Journal Full-text)

Species and tissue-specific isozymes of phosphorylase display differences in regulatory properties consistent with their distinct roles in particular organisms and tissues. In this review, we compare crystallographic structures of regulated and unregulated phosphorylases, including maltodextrin phosphorylase (MalP) from Escherichia coli, glycogen phosphorylase from yeast, and mammalian isozymes from muscle and liver tissues. Mutagenesis and functional studies supplement the structural work and provide insights into the structural basis for allosteric control mechanisms. MalP, a simple, unregulated enzyme, is contrasted with the more complicated yeast and mammalian phosphorylases that have evolved regulatory sites onto the basic catalytic architecture. The human liver and muscle isozymes show differences structurally in their means of invoking allosteric activation. Phosphorylation, though common to both the yeast and mammalian enzymes, occurs at different sites and activates the enzymes by surprisingly different mechanisms.

Molecular Pathway Annotations    
Objects Annotated

Genes (Rattus norvegicus)
Pygb  (glycogen phosphorylase B)
Pygl  (glycogen phosphorylase L)
Pygm  (glycogen phosphorylase, muscle associated)

Genes (Mus musculus)
Pygb  (brain glycogen phosphorylase)
Pygl  (liver glycogen phosphorylase)
Pygm  (muscle glycogen phosphorylase)

Genes (Homo sapiens)
PYGB  (glycogen phosphorylase B)
PYGL  (glycogen phosphorylase L)
PYGM  (glycogen phosphorylase, muscle associated)

Additional Information