Candidapepsin

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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[edit]

  1. ^ Remold, H.; Fasold, H.; Staib, F. (1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochim. Biophys. Acta. 167: 399–406. PMID 5729955. doi:10.1016/0005-2744(68)90219-2. 
  2. ^ Rüchel, R. (1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochim. Biophys. Acta. 659: 99–113. PMID 7018586. doi:10.1016/0005-2744(81)90274-6. 
  3. ^ 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. PMID 6203988. doi:10.1111/1523-1747.ep12261656. 
  4. ^ 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. PMC 331855Freely accessible. PMID 2646602. doi:10.1093/nar/17.4.1779. 

External links[edit]