EXPLOITATION OF SUBTILISIN BPN' AS CATALYST FOR THE SYNTHESIS OF PEPTIDES CONTAINING NONCODED AMINO-ACIDS, PEPTIDE MIMETICS AND PEPTIDE CONJUGATES

The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, pep tide mimetics, and peptide conjugates in a kinetic approach was explor ed. It was found that the enzyme accepts numerous of these types of co mpounds both as acyl donor and acyl acceptor. The results together wit h specificity studies reported by others provide an active site model as a guideline in the design of enzymatic synthesis of biologically im portant compounds.