Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase

• Published in: FEBS letters 1992-03, Vol.299 (3), p.291-293
• Main Authors: Kessler, Efrat, Safrin, Mary, Peretz, Moshe, Burstein, Yigal
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; cleavage; Elastase; Enzyme Precursors - genetics; Enzyme Precursors - metabolism; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; identification; Molecular Sequence Data; Pancreatic Elastase - genetics; Pancreatic Elastase - metabolism; precursors; preproelastase; Preproelastase processing; Protein Processing, Post-Translational; Protein Sorting Signals - chemistry; proteolysis; Proteolytic processing; Pseudomonas aeruginosa; Pseudomonas aeruginosa - enzymology; sites
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80134-3

The extracellular elastase (33 kDa) or Pseudomonas aeruginosa is synthesized as a 53.6 kDa preproenzyme containing a long, N-terminal propeptide. The free propeptide and the elastase precursor generated upon propeptide removal were isolated from P. aeruginosa cells and subjected to N-terminal amino acid sequence analysis. The results identified Ala −174 and Ala +1 as the amino terminal residues of the propeptide and the elastase precursor, respectively, indicating that: (1) the signal peptide consists of 23 amino acid residues and its molecular weight is 2.4 kDa, (2) the propeptide contains 174 amino acid residues and is of 18.1 kDa molecular weight, and (3) no additional N-terminal proteolytic cleavage is required for elastase maturation.