Open AccessA micromolar O‐sulfated thiohydroximate inhibitor bound to plant myrosinase
Author(s) -
Besle Arthur,
Brazzolotto Xavier,
Tatibouët Arnaud,
Cerniauskaite Deimante,
Gallienne Estelle,
Rollin Patrick,
Burmeister Wim P.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109052865
Subject(s) - myrosinase , sinapis , chemistry , stereochemistry , binding site , enzyme , sulfation , biochemistry , biology , glucosinolate , botany , brassica
The 1.6 Å resolution structure of the micromolar competitive inhibitor S ‐( N , N ‐dimethylaminoethyl) phenylacetothiohydroximate‐ O ‐sulfate bound to Sinapis alba myrosinase, a plant thioglucosidase, is reported. Myrosinase and its substrates, the glucosinolates, are part of the plant's defence system. The sulfate group and the phenyl group of the inhibitor bind to the aglycon‐binding site of the enzyme, whereas the N , N ‐dimethyl group binds to the glucose‐binding site and explains the large improvement in binding affinity compared with previous compounds. The structure suggests ways to increase the potency and specificity of the compound by improving the interactions with the hydrophobic pocket of the aglycon‐binding site.