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Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley b-amylasew

DOI: 10.1039/c0mb00204f DOI Help
PMID: 21085740 PMID Help

Authors: Martin Rejzek (John Innes Centre) , Clare Stevenson (John Innes Centre) , Andrew Southard (John Innes Centre) , Duncan Stanley (John Innes Centre) , Kay Denyer (John Innes Centre) , Alison Smith (John Innes Centre) , Mike Naldrett (John Innes Centre) , David Lawson (John Innes Centre) , Robert A. Field (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Biosystems

State: Published (Approved)
Published: October 2010

Abstract: There are major issues regarding the proposed pathway for starch degradation in germinating cereal grain. Given the commercial importance but genetic intractability of the problem, we have embarked on a program of chemical genetics studies to identify and dissect the pathway and regulation of starch degradation in germinating barley grains. As a precursor to in vivo studies, here we report systematic analysis of the reversible and irreversible inhibition of the major b-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley b-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors a-epoxypropyl and a-epoxybutyl glucosides, which target the enzyme’s catalytic residues, and the aglycone site binders acarbose and acyclodextrin.

Journal Keywords: Crystallography; X-Ray; Endosperm; Enzyme; Models; Molecular; Starch; Stereoisomerism; Structure-Activity; beta-Amylase

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Added On: 01/02/2011 16:18

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