|2xfr, resolution 0.97Å ()|
|Related:||2xg9, 2xfy, 2xgb, 2xgi, 2xff, 1b1y|
Crystal structure of barley beta-amylase at atomic resolution
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 beta-amylase of the grain endosperm (BMY1). The molecular basis of inhibitor action was defined through high resolution X-ray crystallography studies of unliganded barley beta-amylase, as well as its complexes with glycone site binder disaccharide iminosugar G1M, irreversible inhibitors alpha-epoxypropyl and alpha-epoxybutyl glucosides, which target the enzyme's catalytic residues, and the aglycone site binders acarbose and alpha-cyclodextrin.
Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley beta-amylase., Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA, Mol Biosyst. 2010 Nov 18. PMID:21085740
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.