THE PRIMARY STRUCTURE OF PEPSTATIN-INSENSITIVE CARBOXYL PROTEINASE PRODUCED BY PSEUDOMONAS SP NO-101

A unique carboxyl proteinase [EC 3.4.23.33] from Pseudomonas sp, No, 1 01 is the first example of a prokaryotic enzyme which is insensitive t o the classical inhibitor, pepstatin, The primary structure of the pro teinase was determined by conventional methods, Pseudomonas carboxyl p roteinase consists of 370 amino acid residues with one disulfide bond, This enzyme has no homologous sequence with any other known carboxyl proteinase, including carboxyl proteinase B from Scytabidium lignicolu m, which is a pepstatin-insensitive carboxyl proteinase. In addition, Pseudomonas carboxyl proteinase lacks the Asp-Thr-Gly, Glu*-Thr-Gly, and Asp-Thr-Ser-Gly (*indicates the catalytic residue) sequences whic h are known as the motif sequences around a pair of catalytic residues in carboxyl proteinases reported so far, The results strongly indicat e that Pseudomonas carboxyl proteinase is a new type of carboxyl prote inase.