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2. Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase

Author

David M. Lawson, Clare E. M. Stevenson, Alison M. Smith, Andrew M. Southard, Kay Denyer, Martin Rejzek, Robert A. Field, Mike J. Naldrett, and Duncan Stanley

Subjects
Models, Molecular, Starch, Molecular Conformation, Disaccharide, Iminosugar, beta-Amylase, Biology, Crystallography, X-Ray, Endosperm, Structure-Activity Relationship, chemistry.chemical_compound, Amylase, Enzyme Inhibitors, Molecular Biology, chemistry.chemical_classification, food and beverages, Stereoisomerism, Aglycone, Enzyme, chemistry, Biochemistry, biology.protein, Edible Grain, Chemical genetics, Biotechnology
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 β-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley β-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors α-epoxypropyl and α-epoxybutyl glucosides, which target the enzyme's catalytic residues, and the aglycone site binders acarbose and α-cyclodextrin.

Published
2011

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