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 |