| IED ID | IndEnz0002000574 |
| Enzyme Type ID | protease000574 |
| Protein Name |
Aspergillopepsin-1 EC 3.4.23.18 Aspartic protease 2 AOAP Aspergillopepsin I Aspergillopeptidase A |
| Gene Name | pepA |
| Organism | Aspergillus oryzae (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) |
| Enzyme Sequence | MVNTSLLAALTAYAVAVSAAPTAPQVKGFSVNQVAVPKGVYRHPAAQLAKAYGKYHATVPTQVAAAAAATGSVTTNPTSNDEEYITQVTVGDDTLGLDFDTGSADLWVFSSQTPSSERSGHDYYTPGSSAQKIDGATWSISYGDGSSASGDVYKDKVTVGGVSYDSQAVESAEKVSSEFTQDTANDGLLGLAFSSINTVQPTPQKTFFDNVKSSLSEPIFAVALKHNAPGVYDFGYTDSSKYTGSITYTDVDNSQGFWGFTADGYSIGSDSSSDSITGIADTGTTLLLLDDSIVDAYYEQVNGASYDSSQGGYVFPSSASLPDFSVTIGDYTATVPGEYISFADVGNGQTFGGIQSNSGIGFSIFGDVFLKSQYVVFDASGPRLGFAAQA |
| Enzyme Length | 390 |
| Uniprot Accession Number | P0CU33 |
| Absorption | |
| Active Site | ACT_SITE 100; /evidence="ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000305|PubMed:12595261"; ACT_SITE 281; /evidence="ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000305|PubMed:12595261" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the microbial peptide pepstatin. {ECO:0000305|PubMed:12595261}. |
| 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:0000250|UniProtKB:Q12567}; |
| 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. {ECO:0000250|UniProtKB:Q12567}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (25); Chain (1); Domain (1); Glycosylation (1); Helix (9); Propeptide (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Aspartyl protease;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8540376}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1IZD; 1IZE; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,551 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |