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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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IntEnzIntEnz view
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Pseudolysin (EC 3.4.24.26, Pseudomonas elastase, Pseudomonas aeruginosa neutral metalloproteinase) is an enzyme.[1][2][3][4][5] 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.