Εμφάνιση απλής εγγραφής

dc.creatorKyriakis, E.en
dc.creatorStravodimos, G. A.en
dc.creatorKantsadi, A. L.en
dc.creatorChatzileontiadou, D. S. M.en
dc.creatorSkamnaki, V. T.en
dc.creatorLeonidas, D. D.en
dc.date.accessioned2015-11-23T10:37:14Z
dc.date.available2015-11-23T10:37:14Z
dc.date.issued2015
dc.identifier10.1016/j.febslet.2015.05.013
dc.identifier.issn0014-5793
dc.identifier.urihttp://hdl.handle.net/11615/30096
dc.description.abstractWe present a study on the binding of gallic acid and its dimer ellagic acid to glycogen phosphorylase (GP). Ellagic acid is a potent inhibitor with K(i)s of 13.4 and 7.5 mu M, in contrast to gallic acid which displays K(i)s of 1.7 and 3.9 mM for GPb and GPa, respectively. Both compounds are competitive inhibitors with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. However, only ellagic acid functions with glucose in a strongly synergistic mode. The crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes were determined at high resolution, revealing that both ligands bind to the inhibitor binding site of the enzyme and highlight the structural basis for the significant difference in their inhibitory potency. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en
dc.source.uri<Go to ISI>://WOS:000358096200013
dc.subjectFlavonoidsen
dc.subjectEllagic aciden
dc.subjectGallic aciden
dc.subjectGlycogen phosphorylaseen
dc.subjectType 2en
dc.subjectdiabetesen
dc.subjectEnzyme inhibitionen
dc.subjectX-ray crystallographyen
dc.subjectINHIBITOR SITEen
dc.subjectCRYSTALLOGRAPHYen
dc.subjectFLAVOPIRIDOLen
dc.subjectDERIVATIVESen
dc.subjectMETABOLISMen
dc.subjectPRODUCTSen
dc.subjectCAFFEINEen
dc.subjectGLUCOSEen
dc.subjectTARGETen
dc.subjectBiochemistry & Molecular Biologyen
dc.subjectBiophysicsen
dc.subjectCell Biologyen
dc.titleNatural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase ben
dc.typejournalArticleen


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