Pseudolysin

Pseudolysin
Identifiers
EC number 3.4.24.26
CAS number 171715-23-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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, J.C. (1980). "Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand". J. Biol. Chem. 255: 3482–3486. PMID 6767718.
  3. Dreyfus, L.A.; Iglewski, B.H. (1986). "Purification and characterization of an extracellular protease of Legionella pneumophila". Infect. Immun. 70: 736–743. PMID 3512431.
  4. Bever, R.A.; Iglewski, B.H. (1988). "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene". J. Bacteriol. 170: 4309–4314. PMID 2842313.
  5. Black, W.J.; Quinn, F.D.; Tompkins, L.S. (1990). "Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase". J. Bacteriol. 172: 2608–2613. PMID 2110146.
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