| IED ID | IndEnz0002018824 |
| Enzyme Type ID | protease018824 |
| Protein Name |
Bradykinin-potentiating peptide S4,1,2 BPP Angiotensin-converting enzyme inhibitor |
| Gene Name | |
| Organism | Bothrops insularis (Golden lancehead) (Lachesis insularis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Bothrops Bothrops insularis (Golden lancehead) (Lachesis insularis) |
| Enzyme Sequence | QGGPPRPQIPP |
| Enzyme Length | 11 |
| Uniprot Accession Number | P30424 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: This peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Modified residue (1); Peptide (1) |
| Keywords | Direct protein sequencing;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:2386615 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,143 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |