Abstract
For ( S)-thiirancarboxylic acid a second-order rate constant of k 2nd=222 M −1 min −1 for the irreversible inhibition of papain was determined. The ethyl and methyl ester do not inhibit the enzyme time-dependently. An improved synthesis of enantiomerically pure thiirancarboxylic acid is described. It is shown that thiirancarboxylates can be substrates for serine proteases (α-chymotrypsin) and esterases (pig liver esterase) and even for metallo proteases (thermolysin).
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