| IED ID | IndEnz0002000570 |
| Enzyme Type ID | protease000570 |
| Protein Name |
Aspergillopepsin-1 EC 3.4.23.18 Acid protease A2 Aspartic protease pepA Aspergillopepsin I Aspergillopepsin O PEPO Aspergillopeptidase A PEPA |
| Gene Name | pepA pepO AO090120000474 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MVILSKVAAVAVGLSTVASALPTGPSHSPHARRGFTINQITRQTARVGPKTASFPAIYSRALAKYGGTVPAHLKSAVASGHGTVVTSPEPNDIEYLTPVNIGGTTLNLDFDTGSADLWVFSEELPKSEQTGHDVYKPSGNASKIAGASWDISYGDGSSASGDVYQDTVTVGGVTAQGQAVEAASKISDQFVQDKNNDGLLGLAFSSINTVKPKPQTTFFDTVKDQLDAPLFAVTLKYHAPGSYDFGFIDKSKFTGELAYADVDDSQGFWQFTADGYSVGKGDAQKAPITGIADTGTTLVMLDDEIVDAYYKQVQGAKNDASAGGYVFPCETELPEFTVVIGSYNAVIPGKHINYAPLQEGSSTCVGGIQSNSGLGLSILGDVFLKSQYVVFDSQGPRLGFAAQA |
| Enzyme Length | 404 |
| Uniprot Accession Number | Q06902 |
| Absorption | |
| Active Site | ACT_SITE 111; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 293; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by sodium lauryl sulfonate. {ECO:0000269|PubMed:8138}. |
| 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:8138}; |
| 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. Hydrolyzes bovine chymotrysinogen A between positions 'Arg-15' and 'Ile-16'. {ECO:0000269|PubMed:239702}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0-4.2. {ECO:0000269|PubMed:8138}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8138}. |
| Modified Residue | |
| Post Translational Modification | PTM: Two isozymes of this enzyme exist which differ only by their non-covalent association with carbohydrate. {ECO:0000305|PubMed:8138}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,313 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.064 mM for Z-His-Phe-Phe-OEt {ECO:0000269|PubMed:239702}; KM=0.037 mM for Z-Ala-Ala-Phe-Phe-OPy4Pr {ECO:0000269|PubMed:239702}; KM=0.1 mM for bovine trypsinogen {ECO:0000269|PubMed:239702}; KM=0.18 mM for bovine chymotrysinogen A {ECO:0000269|PubMed:239702}; Note=kcat is 1.65 sec(-1) with Z-His-Phe-Phe-OEt as substrate, 0.35 sec(-1) with Z-Ala-Ala-Phe-Phe-OPy4Pr as substrate, 13 sec(-1) with bovine trypsinogen as substrate and 1.14 sec(-1) with bovine chymotrysinogen A as substrate. {ECO:0000269|PubMed:239702}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.18; |