| IED ID | IndEnz0002003016 |
| Enzyme Type ID | protease003016 |
| Protein Name |
Aspartyl aminopeptidase DAP EC 3.4.11.21 |
| Gene Name | dapA AO090005001447 |
| 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 | MTSKIAQNLKQPALDFLSFVNASPTPFHAVQSAKELLSKAGFQEIKEKDSWSSTCRPGGKYYLTRNSSTIVAFAIGKKWKPGNPISMIGAHTDSPVLRIKPVSNKRGEGFVQVGVETYGGGIWHTWFDRDLGVAGRAMVRTGDGSIVQKLVKIDRPILRIPTLAIHLDRQETFAFNKETQLFPIAGLVAAELNRTADSTATGEKTAANNETEKGDFAPLKSVTERHHPYLVELIAAEAGVKPDDILDFEMILFDTQKSCLGGLLEEFVFSPRLDNLNSSFCATVGLIDSVADASALDDEPSIRLIALFDHEEIGSRTAQGADSNVLPAIIRRLSVLPSSTSGNEDLATAFEETLSTSFLLSADMAHAVHPNYAAKYENDHRPEINKGPVIKINANARYATNSPGIVLLQEVARKAAEDGGEGVPLQLFVVRNDSSCGSTIGPMLSAALGARTLDLGNPQLSMHSIRETGGTYDVGHSIRLFTSFFKHYSNTSKTIFVD |
| Enzyme Length | 498 |
| Uniprot Accession Number | Q2UPZ7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by zinc. Stimulated by calcium and bacitracin. {ECO:0000269|PubMed:18828788}. |
| Binding Site | BINDING 166; /note=Substrate; /evidence=ECO:0000250; BINDING 311; /note=Substrate; /evidence=ECO:0000250; BINDING 363; /note=Substrate; /evidence=ECO:0000250; BINDING 366; /note=Substrate; /evidence=ECO:0000250; BINDING 391; /note=Substrate; /evidence=ECO:0000250; BINDING 398; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.; EC=3.4.11.21; Evidence={ECO:0000269|PubMed:18828788}; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:17928682, ECO:0000269|PubMed:18828788}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17928682, ECO:0000269|PubMed:18828788}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,992 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.78 mM for Asp-pNA {ECO:0000269|PubMed:17928682, ECO:0000269|PubMed:18828788}; KM=0.068 mM for angiotensin II {ECO:0000269|PubMed:17928682, ECO:0000269|PubMed:18828788}; |
| Metal Binding | METAL 91; /note=Zinc 1; /evidence=ECO:0000250; METAL 274; /note=Zinc 1; /evidence=ECO:0000250; METAL 274; /note=Zinc 2; /evidence=ECO:0000250; METAL 312; /note=Zinc 2; /evidence=ECO:0000250; METAL 363; /note=Zinc 1; /evidence=ECO:0000250; METAL 463; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.21; |