| Candidapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.24 | ||||||||
| CAS no. | 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 is present in yeast Candida albicans.
- ^ Remold H, Fasold H, Staib F (October 1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 167 (2): 399–406. doi: 10.1016/0005-2744(68)90219-2. PMID 5729955.
- ^ Rüchel R (May 1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 659 (1): 99–113. doi: 10.1016/0005-2744(81)90274-6. PMID 7018586.
- ^ Negi M, Tsuboi R, Matsui T, Ogawa H (July 1984). "Isolation and characterization of proteinase from Candida albicans: substrate specificity". The Journal of Investigative Dermatology. 83 (1): 32–6. doi: 10.1111/1523-1747.ep12261656. PMID 6203988.
- ^ Lott TJ, Page LS, Boiron P, Benson J, Reiss E (February 1989). "Nucleotide sequence of the Candida albicans aspartyl proteinase gene". Nucleic Acids Research. 17 (4): 1779. doi: 10.1093/nar/17.4.1779. PMC 331855. PMID 2646602.
- Candidapepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Candidapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.24 | ||||||||
| CAS no. | 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 is present in yeast Candida albicans.
- ^ Remold H, Fasold H, Staib F (October 1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 167 (2): 399–406. doi: 10.1016/0005-2744(68)90219-2. PMID 5729955.
- ^ Rüchel R (May 1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 659 (1): 99–113. doi: 10.1016/0005-2744(81)90274-6. PMID 7018586.
- ^ Negi M, Tsuboi R, Matsui T, Ogawa H (July 1984). "Isolation and characterization of proteinase from Candida albicans: substrate specificity". The Journal of Investigative Dermatology. 83 (1): 32–6. doi: 10.1111/1523-1747.ep12261656. PMID 6203988.
- ^ Lott TJ, Page LS, Boiron P, Benson J, Reiss E (February 1989). "Nucleotide sequence of the Candida albicans aspartyl proteinase gene". Nucleic Acids Research. 17 (4): 1779. doi: 10.1093/nar/17.4.1779. PMC 331855. PMID 2646602.
- Candidapepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)