Inhibitory stereochemistry of N-chloroacetyl-N-hydroxyleucine methyl ester for thermolysin

The previously reported irreversible inhibition of thermolysin by methyl ester, an active site directed inactivator, is found to be due to the -enantiomer. Thus, while the -enantiomer inactivated the enzyme, no inhibitory activity was found with the -enantiomer. A possible explanation is presented for the reversed stereochemistry in the inactivation reaction compared with that of substrate.