Candidapepsin

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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
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NCBI proteins

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 .

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<span class="mw-page-title-main">Sedolisin</span>

The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.

References

  1. 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.
  2. 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.
  3. 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.
  4. 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.