Rather, the enzyme shifts two hydrogen atoms from one carbon atom of the methylglyoxal to the adjacent carbon atom. (wikipedia.org)
As the thiolate anion is not energetically favoured in the hydrophobic interior of the enzyme, it swings into the active site where it can be stabilized by the His202 imidazolium and the dipole of helix C. The Cys123 thiolate which now lies adjacent to the acyl carbon of the substrate, is thus generated only in the presence of substrate. (inrae.fr)
Common3
The 2,3-dihydrobenzofuran derivative, 7-acetyl-4,6-dimethoxy-2-isopropenyl-2,3-dihydrobenzofuran, had an ED 50 value of 1.3 μg (5.4×10 -9 mol)/cm 2 against the common cutworm. (go.jp)
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