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
Full text not available from this repository. (Request a copy)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 |
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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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