| IED ID | IndEnz0002003017 |
| Enzyme Type ID | protease003017 |
| Protein Name |
Aspartyl aminopeptidase 4 EC 3.4.11.21 |
| Gene Name | APE4 YHR113W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MFRIQLRTMSSKTCKSDYPKEFVSFLNSSHSPYHTVHNIKKHLVSNGFKELSERDSWAGHVAQKGKYFVTRNGSSIIAFAVGGKWEPGNPIAITGAHTDSPALRIKPISKRVSEKYLQVGVETYGGAIWHSWFDKDLGVAGRVFVKDAKTGKSIARLVDLNRPLLKIPTLAIHLDRDVNQKFEFNRETQLLPIGGLQEDKTEAKTEKEINNGEFTSIKTIVQRHHAELLGLIAKELAIDTIEDIEDFELILYDHNASTLGGFNDEFVFSGRLDNLTSCFTSMHGLTLAADTEIDRESGIRLMACFDHEEIGSSSAQGADSNFLPNILERLSILKGDGSDQTKPLFHSAILETSAKSFFLSSDVAHAVHPNYANKYESQHKPLLGGGPVIKINANQRYMTNSPGLVLVKRLAEAAKVPLQLFVVANDSPCGSTIGPILASKTGIRTLDLGNPVLSMHSIRETGGSADLEFQIKLFKEFFERYTSIESEIVV |
| Enzyme Length | 490 |
| Uniprot Accession Number | P38821 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The metalloproteases inhibitors EDTA and 1.10-phenanthroline both inhibit the activity, whereas bestatin, an inhibitor of most aminopeptidases, does not affect enzyme activity. {ECO:0000269|PubMed:16367759}. |
| Binding Site | BINDING 173; /note=Substrate; /evidence=ECO:0000250; BINDING 308; /note=Substrate; /evidence=ECO:0000250; BINDING 362; /note=Substrate; /evidence=ECO:0000250; BINDING 365; /note=Substrate; /evidence=ECO:0000250; BINDING 390; /note=Substrate; /evidence=ECO:0000250; BINDING 397; /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; |
| DNA Binding | |
| EC Number | 3.4.11.21 |
| Enzyme Function | FUNCTION: Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation. {ECO:0000269|PubMed:16367759}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.9. {ECO:0000269|PubMed:16367759}; |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Vacuole;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21343297}. Vacuole lumen {ECO:0000269|PubMed:17651441, ECO:0000269|PubMed:21343297}. Note=In growing conditions, a small portion localizes in the vacuole, but actively transported to the vacuole under nutrient starvation conditions. {ECO:0000269|PubMed:21343297}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11283351; 15606766; 16429126; 16702403; 18719252; 19536198; 22489171; 23217712; 25549323; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,174 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for angiotensin I {ECO:0000269|PubMed:16367759}; |
| Metal Binding | METAL 97; /note=Zinc 1; /evidence=ECO:0000250; METAL 273; /note=Zinc 1; /evidence=ECO:0000250; METAL 273; /note=Zinc 2; /evidence=ECO:0000250; METAL 309; /note=Zinc 2; /evidence=ECO:0000250; METAL 362; /note=Zinc 1; /evidence=ECO:0000250; METAL 456; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |