Staphopain (EC 3.4.22.48, staphylopain) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
| Staphopain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.48 | ||||||||
| CAS no. | 347841-89-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates.
This enzyme is present in several species of Staphylococcus.
References
edit- ^ Hofmann, B.; Hecht, H.J.; Kiess, M.; Schomburg, D. (1993). "Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex". Acta Crystallographica Section A. 49: c102. doi:10.1107/s0108767378097081.
- ^ Potempa J, Dubin A, Travis J (1998). "Staphylopain". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 669–671.
- ^ Dubin G, Chmiel D, Mak P, Rakwalska M, Rzychon M, Dubin A (November 2001). "Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis". Biological Chemistry. 382 (11): 1575–82. doi:10.1515/bc.2001.192. PMID 11767947.
External links
edit- Staphopain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
