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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
PMID:
21085740
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 enzymes 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
Diamond Keywords: Cereal Crops; Enzymes
Subject Areas:
Biology and Bio-materials
Instruments:
I02-Macromolecular Crystallography
Other Facilities: PX10.1 at SRS
Added On:
01/02/2011 16:18
Discipline Tags:
Plant science
Agriculture & Fisheries
Genetics
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)