Modification of porcine carboxypeptidase B with [14C]-bromoacetyl-p-aminobenzylsuccinic acid results in a marked decrease of the activity toward both peptide and ester substrates. The inactivation correlates with the incorporation of 1 equivalent of inhibitor molecule per carboxypeptidase molecule. Evidence is presented that inactivation is due to alkylation of a single, presumably methionyl residue in the active center of the enzyme.
|Number of pages||9|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 18 Jun 1974|