| IED ID | IndEnz0002016785 |
| Enzyme Type ID | protease016785 |
| Protein Name |
Subtilisin-like serine protease AS-E2 EC 3.4.21.- Fragment |
| Gene Name | |
| Organism | Acremonium sp. |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreales incertae sedis Acremonium unclassified Acremonium Acremonium sp. |
| Enzyme Sequence | AYVSQSGAPWGLGRISHK |
| Enzyme Length | 18 |
| Uniprot Accession Number | P85157 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by antipain, PMSF and aprotinin. Inhibited by benzamidine by 49%. Little or no inhibition by EDTA, E-64, iodoacetic acid, leupeptin and FUT-175. {ECO:0000269|PubMed:17482570}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Subtilisin-like serine protease. Cleaves prothrombin at 151-Ala-|-Met-152, 271-Arg-|-Thr-272 and 316-Tyr-|-Ile-317 to produces meizothrombin(desF1)-like molecules. Degrades fibinogen. Inhibits plasma coagulation. {ECO:0000269|PubMed:17482570}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:17482570}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:17482570}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Hydrolase;Protease;Prothrombin activator;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,914 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |