| IED ID | IndEnz0002000619 |
| Enzyme Type ID | protease000619 |
| Protein Name |
Penicillopepsin-1 EC 3.4.23.20 Acid protease Aspartic protease aspA |
| Gene Name | aspA |
| Organism | Penicillium roqueforti |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium roqueforti |
| Enzyme Sequence | MVVFSQVTVALTCFSAIASAAAVRQEPPQGFTVNQVQKAVPGTRTVNLPGLYANALVKYGATVPATVHAAAVSGSAITTPEADDVEYLTPVTIGSSTLNLDFDTGSADLWVFSSELTSSQQSGHDVYNVGSLGTKLSGASWSISYGDGSSASGDVYKDTVTVGGVKATGQAVEAAKKISSQFLQDKNNDGLLGMAFSSINTVSPTPQKTFFDTVKSSLGEPLFAVTLQGTGRPWHLRFGYIDSDKYTGTLAYADVDDSDGFWSFTADSYKIGTGAAGKSITGIADTGTTLLLLDSSIVTGLLQEGYPGSQNSSSAGGYIFPCSATLPDFTVTINGYDAVVPGKYINFAPVSTGSSSCYGGIQSNSGIGFSIFGDIFLKSQYVVFDSEGPRLGFAAQA |
| Enzyme Length | 397 |
| Uniprot Accession Number | Q01972 |
| Absorption | |
| Active Site | ACT_SITE 103; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 285; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.; EC=3.4.23.20; Evidence={ECO:0000269|PubMed:4790849}; |
| DNA Binding | |
| EC Number | 3.4.23.20 |
| Enzyme Function | FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'. {ECO:0000269|PubMed:4790849, ECO:0000269|PubMed:9413440}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:4790849}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5. {ECO:0000269|PubMed:4790849}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Repressed by alkaline pH and in presence of ammonia. {ECO:0000269|PubMed:9413440}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9413440}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,112 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |