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 |