Aureolysin
| Aureolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.29 | ||||||||
| CAS number | 39335-13-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aureolysin (EC 3.4.24.29, Staphylococcus aureus neutral proteinase, Staphylococcus aureus neutral protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
This metalloenzyme is present in S. aureus.
References
- ↑ Arvidson, S. (1973). "Studies on extracellular proteolytic enzymes from Staphylococcus aureus'. II. Isolation and characterization of an EDTA-sensitive protease". Biochim. Biophys. Acta. 302: 149–157. doi:10.1016/0005-2744(73)90017-x. PMID 4632563.
- ↑ Saheb, S.A. (1976). "Purification et caractérisation d’une protéase extracellulaire de Staphylococcus aureus inhibée par l’E.D.T.A". Biochimie. 58: 793–804. doi:10.1016/s0300-9084(76)80310-0. PMID 823980.
- ↑ Drapeau, G.R. (1978). "Role of a metalloprotease in activation of the precursor of staphylococcal protease". J. Bacteriol. 136: 607–613. PMID 711676.
- ↑ Potempa, J.; Porwit-Bohr, Z.; Travis, J. (1989). "Stabilization vs. degradation of Staphylococcus aureus' metalloproteinase". Biochim. Biophys. Acta. 993: 301–304. doi:10.1016/0304-4165(89)90181-5. PMID 2512988.
External links
- Aureolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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