The primary structure of staphylococcal protease

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Abstract
The amino acid sequence of staphylococcal protease was determined by analysis of tryptic peptides obtained from CNBr fragments. Selected peptides obtained from digests with staphylococcal protease, thermolysin and chymotrypsin provided the information necessary to align the tryptic peptides and the CNBr fragments. The protease is a single polypeptide chain of some 250 amino acids and is devoid of SH groups. The COOH-terminal tryptic peptide of the protease molecule contains more 43 residues, most of which are aspartic acids, asparagines and prolines. The amino acid sequence of this peptide was not determined. The primary structure near the active serine residue indicates that staphylococcal protease is related to the pancreatic serine proteases. It has little or no additional sequence homologies with these enzymes except for the regions near histidine-50 and aspartic acid-91. These regions have striking similarities with the corresponding regions of protease B and the trypsin-like enzyme of Streptomyces griseus.

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