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

Rejzek, Martin, Stevenson, Clare E., Southard, Andrew M., Stanley, Duncan, Denyer, Kay, Smith, Alison M., Naldrett, Mike J., Lawson, David M. and Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 (2011) Chemical genetics and cereal starch metabolism:Structural basis of the non-covalent and covalent inhibition of barley β-amylase. Molecular BioSystems, 7 (3). pp. 718-730. ISSN 1742-206X

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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.

Item Type: Article
Uncontrolled Keywords: biotechnology,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1305
Faculty \ School:
Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 06 Sep 2024 13:34
Last Modified: 25 Sep 2024 18:07
URI: https://ueaeprints.uea.ac.uk/id/eprint/96586
DOI: 10.1039/c0mb00204f

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