| IED ID | IndEnz0002005905 |
| Enzyme Type ID | protease005905 |
| Protein Name |
Candidapepsin-8 EC 3.4.23.24 ACP 8 Aspartate protease 8 Secreted aspartic protease 8 |
| Gene Name | SAP8 CAALFM_C302510CA CaO19.242 CaO19.7872 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MVSIITFTKNVLVTLAFALLAQGLAIPEDIDKRAEKVVSLDFTVTRKPFNATAHGQHHQSQQQQQQQQQQPAQKRGTVQTSLINEGPSYAATITVGSNKQQQTVIVDTGSSDLWVVDSAAVCQVTYPGQSPTFCKQDGTYKPSSSTTSQNLGKAFSIRYEDGSSSQGTVYKDTVGLGGASITNQQFADVTTTSVDQGILGIGFTGDESSPTYDNVPVTLKKQGIINKNAYSLYLNSASASSGTIIFGGVDNAKYTGSLTALPITSSNELRVQLSTINIAGTTVSASTTPVLDSGTTLTYFSQTIADKLAAAVGAKWNSYYQLYTSSCNLAGNIVFNFAKGVTISVPLSEFVLQDGNSCYFGVSRDSATILGDNFLRRAYAVYDLDGNTISLAQVKYTTSSSISTL |
| Enzyme Length | 405 |
| Uniprot Accession Number | Q5AEM6 |
| Absorption | |
| Active Site | ACT_SITE 107; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 292; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.; EC=3.4.23.24; Evidence={ECO:0000269|PubMed:21646240}; |
| DNA Binding | |
| EC Number | 3.4.23.24 |
| Enzyme Function | FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Serves as a major regulator of MSB2-processing which activates CEK1 MAPK-signaling affecting biofilm formation and oropharyngeal candidiasis. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein. {ECO:0000269|PubMed:22302440, ECO:0000269|PubMed:23139737, ECO:0000269|PubMed:23927842}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.5. {ECO:0000269|PubMed:21646240}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Propeptide (1); Region (4); Signal peptide (1) |
| Keywords | Aspartyl protease;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers. {ECO:0000269|PubMed:22302440, ECO:0000269|PubMed:9802014}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,037 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.24; |