Biology:Pseudolysin
From HandWiki
| Pseudolysin | |||||||||
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| 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 | ||||||||
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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
- ↑ "Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase". Agric. Biol. Chem. 39: 1123–1128. 1975. doi:10.1271/bbb1961.39.1123.
- ↑ "Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand". The Journal of Biological Chemistry 255 (8): 3482–6. April 1980. PMID 6767718.
- ↑ "Purification and characterization of an extracellular protease of Legionella pneumophila". Infection and Immunity 51 (3): 736–43. March 1986. PMID 3512431.
- ↑ "Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene". Journal of Bacteriology 170 (9): 4309–14. September 1988. PMID 2842313.
- ↑ "Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase". Journal of Bacteriology 172 (5): 2608–13. May 1990. PMID 2110146.
External links
- Pseudolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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