Journal of the American Chemical Society p. 182 - 184 (1981)
Update date:2022-08-28
Topics:
Fried, Herbert E.
Kaiser, E. T.
The redox reactions between flavopapain 1 and various dithiols have been examined under anaerobic conditions.The semisynthetic enzyme is an effective catalyst relative to the model flavin, 7-acetyl-10-methylisoalloxazine (3).Relative rate enhancements, (kcat/Km)/k2model, observed are 3.9, 8.0, and 17.4 for dithiotreitol, d,l-dihydrolipoic acid, and d,l-dihydrolipoamide, respectively.This substrate specificity, also seen in N-alkyl-1,4-dihydronicotinamide series, is explicable in terms of favorable hydrophobic-hydrophobic binding interaction between the substrates and the enzyme active site.Stereospecificity was not observed in the enzymatic reactions of the dithiols.It is demonstrated that the enzyme and model flavin reactions of the dithiols both proceeded via comparable mechanistic pathway.
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