| IED ID | IndEnz0002007494 |
| Enzyme Type ID | protease007494 |
| Protein Name |
Elastase-1 EC 3.4.21.36 |
| Gene Name | |
| Organism | Salmo salar (Atlantic salmon) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Protacanthopterygii Salmoniformes (salmons and trouts) Salmonidae (salmonids) Salmoninae (trouts salmons & chars) Salmo Salmo salar (Atlantic salmon) |
| Enzyme Sequence | VVGGRVAQPNSWPWQISLQYKSGSSYYHTCGGSLIRQGWVMTAAHCVDSARTWRVVLGEHNLNTNEGKEQIMTVNSVFIHSGWNSDDVAGGYDIALLRLNTQASLNSAVQLAALPPSNQILPNNNPCYITGWGKTSTGGPLSDSLKQAWLPSVDHATCSSSGWWGSTVKTTMVCAGGGANSGCNGDSGGPLNCQVNGSYYVHGVTSFVSSSGCNASKKPTVFTRVSAYISWMNGIM |
| Enzyme Length | 236 |
| Uniprot Accession Number | Q7SIG3 |
| Absorption | |
| Active Site | ACT_SITE 45; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15299762; ACT_SITE 93; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15299762; ACT_SITE 187; /note=Charge relay system; /evidence=ECO:0000269|PubMed:15299762 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.; EC=3.4.21.36; Evidence={ECO:0000269|PubMed:9628006}; |
| DNA Binding | |
| EC Number | 3.4.21.36 |
| Enzyme Function | FUNCTION: Acts upon elastin. {ECO:0000269|PubMed:9628006}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1 at 22 degrees Celsius with Suc-AAA-pNA as the substrate. {ECO:0000269|PubMed:9628006}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (1); Disulfide bond (4); Domain (1); Helix (6); Metal binding (5); Turn (1) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9628006}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1ELT; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,015 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.47 mM for Suc-AAA-pNA (at 22 degrees Celsius) {ECO:0000269|PubMed:9628006}; KM=1.34 mM for Suc-AAPL-pNA (at 22 degrees Celsius) {ECO:0000269|PubMed:9628006}; KM=0.82 mM for Suc-AAPV-pNA (at 22 degrees Celsius) {ECO:0000269|PubMed:9628006}; KM=0.83 mM for Suc-AAPA-pNA (at 22 degrees Celsius) {ECO:0000269|PubMed:9628006}; KM=0.15 mM for Suc-AAPI-pNA (at 22 degrees Celsius) {ECO:0000269|PubMed:9628006}; |
| Metal Binding | METAL 59; /note=Calcium; /evidence=ECO:0000269|PubMed:15299762; METAL 61; /note=Calcium; via carbonyl oxygen; METAL 64; /note=Calcium; via carbonyl oxygen; METAL 66; /note=Calcium; /evidence=ECO:0000269|PubMed:15299762; METAL 69; /note=Calcium; /evidence=ECO:0000269|PubMed:15299762 |
| Rhea ID | |
| Cross Reference Brenda |