The primary structure of staphylococcal protease

Area of Science:

• Biochemistry
• Enzymology
• Molecular Biology

Background:

• Staphylococcal protease is an extracellular enzyme produced by Staphylococcus aureus.
• Understanding its structure is crucial for elucidating its function and potential applications.

Purpose of the Study:

• To determine the complete amino acid sequence of staphylococcal protease.
• To investigate its structural relationship with other serine proteases.

Main Methods:

• Peptide mapping using cyanogen bromide fragmentation.
• Enzymatic digestion with staphylococcal protease, thermolysin, and chymotrypsin.
• Amino acid sequencing of resulting peptides.

Main Results:

• The protease consists of a single polypeptide chain of approximately 250 amino acids.
• It lacks sulfhydryl groups.
• Sequence analysis revealed homology to pancreatic serine proteases, particularly near active site residues (histidine-50 and aspartic acid-91).

Conclusions:

• Staphylococcal protease shares structural similarities with pancreatic serine proteases, suggesting a common evolutionary origin.
• Specific homologies indicate functional relevance of conserved regions.
• The determined sequence provides a foundation for further studies on staphylococcal protease structure-function relationships.