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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.
Pubmed: (View Article at PubMed) PMID:11340058
DOI: Full-text: DOI:10.1146/annurev.biophys.30.1.191

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.

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CRRD Object Information
CRRD ID: 1642822
Created: 2007-10-18
Species: All species
Last Modified: 2007-10-18
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.