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Pseudolysin

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Pseudolysin
Identifiers
EC no.3.4.24.26
CAS no.171715-23-4
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Pseudolysin (EC 3.4.24.26, Pseudomonas elastase, Pseudomonas aeruginosa neutral metalloproteinase) is an enzyme. This enzyme catalyses the following chemical 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

This enzyme belongs to the peptidase family M4 (thermolysin family).

References

  1. Morihara K, Tsuzuki H (1975). "Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase". Agric. Biol. Chem. 39: 1123–1128. doi:10.1271/bbb1961.39.1123.
  2. Nishino N, Powers JC (April 1980). "Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand". The Journal of Biological Chemistry. 255 (8): 3482–6. PMID 6767718.
  3. Dreyfus LA, Iglewski BH (March 1986). "Purification and characterization of an extracellular protease of Legionella pneumophila". Infection and Immunity. 51 (3): 736–43. PMC 260959. PMID 3512431.
  4. Bever RA, Iglewski BH (September 1988). "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene". Journal of Bacteriology. 170 (9): 4309–14. PMC 211443. PMID 2842313.
  5. Black WJ, Quinn FD, Tompkins LS (May 1990). "Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase". Journal of Bacteriology. 172 (5): 2608–13. PMID 2110146.

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Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins
Matrix metalloproteinases
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