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Titolo:
Structural relationships among regulated and unregulated phosphorylases
Autore:
Buchbinder, JL; Rath, VL; Fletterick, RJ;
Indirizzi:
Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA Pfizer Inc, Cent Res, Exploratory Med Sci, Groton, CT 06340 USA Pfizer Inc Groton CT USA 06340 Exploratory Med Sci, Groton, CT 06340 USA
Titolo Testata:
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE
, volume: 30, anno: 2001,
pagine: 191 - 209
SICI:
1056-8700(2001)30:<191:SRARAU>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI MALTODEXTRIN PHOSPHORYLASE; LIVER-GLYCOGEN PHOSPHORYLASE; ESCHERICHIA-COLI; CATALYTIC SITE; PROTEIN PHOSPHATASES; SUBSTRATE-BINDING; ALLOSTERIC SITE; ACTIVE-SITE; T-STATE; ACTIVATION;
Keywords:
allosteric; enzymes; molecular structure; site-directed mutagenesis; X-ray diffraction;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Rath, VL Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 CA 94143 USA
Citazione:
J.L. Buchbinder et al., "Structural relationships among regulated and unregulated phosphorylases", ANN R BIO B, 30, 2001, pp. 191-209

Abstract

Species and tissue-specific isozymes of phosphorylase display differences in regulatory properties consistent with their distinct roles in particularorganisms 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 thestructural 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 17:27:14