IED ID | IndEnz0002014192 |
Enzyme Type ID | protease014192 |
Protein Name |
Protease inhibitor AmPI Fragment |
Gene Name | |
Organism | Antheraea mylitta (Tasar silkworm) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Saturniidae (emperor moths) Saturniinae Saturniini Antheraea Antheraea mylitta (Tasar silkworm) |
Enzyme Sequence | AEPLASQLKEPIAGGGWWAA |
Enzyme Length | 20 |
Uniprot Accession Number | P84885 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Inhibits trypsin and chymotrypsin. {ECO:0000269|PubMed:19723549, ECO:0000269|Ref.1}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4-65 degrees Celsius. Activity decreases rapidly at higher temperatures, nearly 40% of activity is retained at 100 degrees Celsius. {ECO:0000269|PubMed:19723549}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-9.0. High activity is also seen over the range pH 2.0-4.5. Activity decreases with increasing pH above pH 9.0. {ECO:0000269|PubMed:19723549}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Non-terminal residue (1) |
Keywords | Direct protein sequencing;Glycoprotein;Protease inhibitor;Serine protease inhibitor |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:19723549, ECO:0000269|Ref.1}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 2,052 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |