| IED ID | IndEnz0002010155 |
| Enzyme Type ID | protease010155 |
| Protein Name |
Serine proteinase EC 3.4.21.- Fragment |
| Gene Name | |
| Organism | Scedosporium boydii (Pseudallescheria boydii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Microascales Microascaceae Scedosporium Scedosporium boydii (Pseudallescheria boydii) |
| Enzyme Sequence | AYTGQTGAPWGLA |
| Enzyme Length | 13 |
| Uniprot Accession Number | Q10721 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by pMSF, chymotrypsin and SDS. Inhibited by the trypsin inhibitors Tos-Phe-CH2Cl, Tos-Lys-CH2Cl and SBTI, and by bivalent cations. Slightly inhibited by the elastitinal and metal chelators EDTA and EGTA, by ethanol and by non-ionic detergents. Not inhibited by alkylating agents, reducing agents, pepstatin, o-phenanthroline, leupeptin, E-64, bestatin, DMSO and methanol. {ECO:0000269|PubMed:8670095}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease. Degrades fibrinogen. {ECO:0000269|PubMed:8670095}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-50 degrees Celsius. 49% of maximum activity is seen at 60 degrees Celsius, no activity is seen at 70 degrees Celsius. Thermolabile, a significant decrease in activity is seen after incubation at temperatures above 42 degrees Celsius for 20 min. {ECO:0000269|PubMed:8670095}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. 20% of maximum activity is seen at pH 5.0. Inactive below pH 5.0 and above pH 11.0, inactivation by acidic pH is reversible. {ECO:0000269|PubMed:8670095}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Hydrolase;Protease;Secreted;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670095}. |
| Modified Residue | |
| Post Translational Modification | PTM: Not glycosylated. {ECO:0000269|PubMed:8670095}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,292 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.35 mM for N-Suc-Ala-Ala-Pro-Phe-pNA {ECO:0000269|PubMed:8670095}; KM=0.31 mM for N-Ac-Ile-Glu-Ala-Arg-pNA {ECO:0000269|PubMed:8670095}; KM=2.59 mM for N-Suc-Ala-Ala-Pro-Leu-pNA {ECO:0000269|PubMed:8670095}; Vmax=1032 umol/min/mg enzyme toward N-Suc-Ala-Ala-Pro-Phe- pNA {ECO:0000269|PubMed:8670095}; Vmax=234 umol/min/mg enzyme toward N-Ac-Ile-Glu-Ala-Arg- pNA {ECO:0000269|PubMed:8670095}; Vmax=613 umol/min/mg enzyme toward N-Suc-Ala-Ala-Pro-Leu- pNA {ECO:0000269|PubMed:8670095}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |