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

FEBS Letters

Kessler, Efrat²  Burstein, Yigal¹  Peretz, Moshe¹  Safrin, Mary² 

[1] Department of Organic Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel;Maurice and Gabriela Goldschleger Eye Research Institute, Tel-Aviv University, Sackler Faculty of Medicine, Sheba Medical Center, Tel-Hashomer 52621, Israel

关键词: Proteolytic processing;    Preproelastase processing;    Elastase;    Pseudomonas aeruginosa;   

DOI  :  10.1016/0014-5793(92)80134-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown