| IED ID | IndEnz0002006800 |
| Enzyme Type ID | protease006800 |
| Protein Name |
Aspartyl aminopeptidase EC 3.4.11.21 |
| Gene Name | dnpp-1 F01F1.9 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MAAALKPSAPEIRKAAQEFINYLNKAVTPFHATQEVKDRLLQAGFTELPESGHWDIQPTSKYFVTKNRSAILAFAVGGSYKPGSGFSIVVGHTDSPCLRVKPISHQKSDKFLQVGVSTYGGGIWRTWFDRDLSVAGLVIVKNGEKLQHKLIDVKKPVLFIPNLAIHLETDRTTFKPNTETELRPILETFAAAGINAPQKPESTGFADPRNITNNHHPQFLGLIAKEAGCQPEDIVDLDLYLYDTNKAAIVGMEDEFISGARLDNQVGTYTAISGLLESLTGESFKNDPQIRIAACFDNEEVGSDSAMGASSSFTEFVLRRLSAGGSTTAFEEAIGKSMLISADQAHATHPNYSAKHEENHRPAFHGGVVVKVNVNQRYATTSTTHAALKQVAFEAQVPLQVVVVRNDSPCGSTVGPILATKLGLQTVDVGCPQLAMHSIREFADTSSIYQATTLYSTFYERLSTVLSNMQ |
| Enzyme Length | 470 |
| Uniprot Accession Number | Q19087 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 166; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 299; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 343; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 346; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 371; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0; BINDING 378; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| 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:23427264}; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Plays a role in membrane trafficking and is specifically involved in the recycling and degradation of endocytic cargo. {ECO:0000269|PubMed:23427264}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Metal binding (6); Mutagenesis (4) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23427264}. Note=Diffuse expression in the cytosol. {ECO:0000269|PubMed:23427264}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11731503; 11997343; 19123269; 21085631; 21177967; 22560298; 23800452; 25487147; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,157 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.58 mM for H-Asp-NHMec (at pH 7.5) {ECO:0000269|PubMed:23427264}; KM=8.854 mM for H-Glu-NHMec (at pH 7.5) {ECO:0000269|PubMed:23427264}; |
| Metal Binding | METAL 92; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 263; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 263; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 300; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 343; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9ULA0; METAL 437; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9ULA0 |
| Rhea ID | |
| Cross Reference Brenda |