Candidapepsin
| Candidapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.24 | ||||||||
| CAS number | 69458-91-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Candidapepsin (EC 3.4.23.24, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida olea acid proteinase, Candida aspartic proteinase, Candida olea aspartic proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin
This endopeptidase js present in yeast Candida albicans.
References
- ↑ Remold, H.; Fasold, H.; Staib, F. (1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochim. Biophys. Acta. 167: 399–406. doi:10.1016/0005-2744(68)90219-2. PMID 5729955.
- ↑ Rüchel, R. (1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochim. Biophys. Acta. 659: 99–113. doi:10.1016/0005-2744(81)90274-6. PMID 7018586.
- ↑ Negi, M.; Tsuboi, R.; Matsui, T.; Ogawa, H. (1984). "Isolation and characterization of proteinase from Candida albicans: substrate specificity". J. Invest. Dermatol. 83: 32–36. doi:10.1111/1523-1747.ep12261656. PMID 6203988.
- ↑ Lott, T.J.; Page, L.S.; Boiron, P.; Benson, J.; Reiss, E. (1989). "Nucleotide sequence of the Candida albicans aspartyl proteinase gene". Nucleic Acids Res. 17: 1779–1779. doi:10.1093/nar/17.4.1779. PMID 2646602.
External links
- Candidapepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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