| IED ID | IndEnz0002000578 |
| Enzyme Type ID | protease000578 |
| Protein Name |
Aspergillopepsin-1 EC 3.4.23.18 Aspartic protease pepA Aspergillopepsin I Aspergillopeptidase A |
| Gene Name | pepA |
| Organism | Aspergillus pseudoglaucus (Eurotium repens) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus pseudoglaucus (Eurotium repens) |
| Enzyme Sequence | MVNTSLLAALTAYAVAVAAAPTAPQVKGFSVNQVAVPKGVYRHPAAQLAKAYGKYHATVPTQVAAAAAATGSVTTNPTSNDEEYITQVTVGDDTLGLDFDTGSADLWVFSSQTPSSERSGHDYYTPGSSAQKIDGATWSISYGDGSSASGDVYKDKVTVGGVSYDSQAVESAEKVSSEFTQDTENDGLLGLAFSSINTVQPTPQKTFFDNVKSSLSEPIFAVALKHNAPGVYDFGYTDSSKYTGSITYTDVDNSQGFWSFTADGYSIGSDSSSDSITGIADTGTTLLLLDDSIVDAYYEQVNGASYDSSQGGYVFPSSASLPDFSVTIGDYTATVPGEYISFADVGNGQTFGGIQSNSGIGFSIFGDVFLKSQYVVFDASGPRLGFAAQA |
| Enzyme Length | 390 |
| Uniprot Accession Number | A0A146F0J0 |
| Absorption | |
| Active Site | ACT_SITE 100; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 281; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the microbial peptide pepstatin A. {ECO:0000269|PubMed:23044751}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.; EC=3.4.23.18; Evidence={ECO:0000269|PubMed:23044751}; |
| DNA Binding | |
| EC Number | 3.4.23.18 |
| 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 also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A (By similarity). Hydrolyzes myoglobin, hemoglobin and other natural proteins. Hydrolyzes equine myoglobin between positions 'Met-1' and 'Gly-2', 'Lys-43' and 'Phe-44', and 'Leu-70' and 'Thr-71' (PubMed:23044751). {ECO:0000250|UniProtKB:Q12567, ECO:0000269|PubMed:23044751}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:23044751}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2-4. Stable from pH 2 to pH 6. {ECO:0000269|PubMed:23044751}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Aspartyl protease;Direct protein sequencing;Hydrolase;Protease;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,623 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for equine myoglobin {ECO:0000269|PubMed:23044751}; KM=7.9 uM for bovine hemoglobin {ECO:0000269|PubMed:23044751}; Note=kcat is 0.05 min(-1) with equine myoglobin as substrate and 0.0646 min(-1) with bovine hemoglobin as substrate. {ECO:0000269|PubMed:23044751}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.18; |