EC 3.4.24.26 - Pseudolysin

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IntEnz Enzyme Nomenclature
EC 3.4.24.26

Names

Accepted name:
pseudolysin
Other names:
Pseudomonas aeruginosa neutral metalloproteinase
Pseudomonas elastase
Systematic name:
-

Reaction

Cofactors

Comments:

In peptidase family M4 (thermolysin family). From the pathogenic bacteria Pseudomonas aeruginosa and Legionella pneumophila, and causes tissue damage. Formerly included in EC 3.4.24.4.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
CAS Registry Number: 171715-23-4
UniProtKB/Swiss-Prot:

References

  1. Morihara, K. and Tsuzuki, H.
    Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase.
    Agric. Biol. Chem. 39: 1123-1128 (1975).
  2. Nishino, N. and Powers, J.C.
    Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand.
    J. Biol. Chem. 255: 3482-3486 (1980). [PMID: 6767718]
  3. Dreyfus, L.A. and Iglewski, B.H.
    Purification and characterization of an extracellular protease of Legionella pneumophila.
    Infect. Immun. 70: 736-743 (1986). [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: 4309-4314 (1988). [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: 2608-2613 (1990). [PMID: 2110146]

[EC 3.4.24.26 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.26]