| EC |
3.4.24.26 |
| Accepted name: |
pseudolysin |
| Reaction: |
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1′. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects |
| Other name(s): |
Pseudomonas elastase; Pseudomonas aeruginosa neutral metalloproteinase |
| Comments: |
In peptidase family M4 (thermolysin family). From the pathogenic bacteria Pseudomonas aeruginosa and Legionella pneumophila, and causes tissue damage. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 171715-23-4 |
| References: |
| 1. |
Morihara, K. and Tsuzuki, H. Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase. Agric. Biol. Chem. 39 (1975) 1123–1128. |
| 2. |
Nishino, N. and Powers, J.C. Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand. J. Biol. Chem. 255 (1980) 3482–3486. [PMID: 6767718] |
| 3. |
Dreyfus, L.A. and Iglewski, B.H. Purification and characterization of an extracellular protease of Legionella pneumophila. Infect. Immun. 70 (1986) 736–743. [PMID: 3512431] |
| 4. |
Bever, R.A. and Iglewski, B.H. Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene. J. Bacteriol. 170 (1988) 4309–4314. [DOI] [PMID: 2842313] |
| 5. |
Black, W.J., Quinn, F.D. and Tompkins, L.S. Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase. J. Bacteriol. 172 (1990) 2608–2613. [DOI] [PMID: 2110146] |
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| [EC 3.4.24.26 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.26] |
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