Jump to main content
Jump to site search

Issue 3, 2011
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation

Supplementary files

Article information


Submitted
21 Sep 2010
Accepted
21 Oct 2010
First published
18 Nov 2010

Mol. BioSyst., 2011,7, 718-730
Article type
Paper

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

M. Rejzek, C. E. Stevenson, A. M. Southard, D. Stanley, K. Denyer, A. M. Smith, M. J. Naldrett, D. M. Lawson and R. A. Field, Mol. BioSyst., 2011, 7, 718
DOI: 10.1039/C0MB00204F

Search articles by author

Spotlight

Advertisements