A micromolar O-sulfated thiohydroximate inhibitor bound to plant myrosinase

作者：Besle Arthur; Brazzolotto Xavier; Tatibouet Arnaud; Cerniauskaite Deimante; Gallienne Estelle; Rollin Patrick; Burmeister Wim P^*

来源：Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2010, 66(2): 152-155.

DOI：10.1107/S1744309109052865

The 1.6 angstrom 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.

• 出版日期2010-2