The Enzyme Database

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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, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 171715-23-4
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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