| IED ID | IndEnz0002005994 |
| Enzyme Type ID | protease005994 |
| Protein Name |
Candidapepsin-2 EC 3.4.23.24 ACP 2 Aspartate protease 2 |
| Gene Name | SAPP2 ACPL |
| Organism | Candida parapsilosis (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida parapsilosis (Yeast) |
| Enzyme Sequence | MTTIAIFTKNVLLAIAFALFAQGAAIPDPAKRDDNPGFVALDFEVTRKPLDVNATSELSKRSSPSSPLYFEGPSYGIRVSVGSNKQEQQVVLDTGSSDFWVVDSSASCQKGNCKQYGTFDPHSSTSFKSLGSSFRSIGYGDKSSSIGTWGQDTIYLGGTSITNQRFADVTSTSVNQGILGVGRVETESANPPYDNVPITLKKQGKIKTNAYSLYLNSPGAATGTIIFGGVDNAKYSGKLIEEPLVSDRYLAVNLKSLNYNGDNSNAGFGVVVDSGTTISYLPDSIVNDLANKVGAYLEPVGLGNELYFIDCNANPQGSASFTFDNGAKITVPLSEFVLQSTANACVWGLQSSDRQNVPPILGDNFLRHAYAFQLDKETVLSRSGEVHFCLKCFSNLETSIVWKAFFYNRYIQ |
| Enzyme Length | 412 |
| Uniprot Accession Number | P32950 |
| Absorption | |
| Active Site | ACT_SITE 93; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 273; /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; |
| DNA Binding | |
| EC Number | 3.4.23.24 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000305}. |
| Signal Peptide | SIGNAL 1..25; /note="Or 18, or 21"; /evidence="ECO:0000255" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,443 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.24; |