| IED ID | IndEnz0002014500 |
| Enzyme Type ID | protease014500 |
| Protein Name |
Bradykinin potentiating and C-type natriuretic peptides BPP-CNP Cleaved into: Bradykinin-potentiating peptide Cdt1a; Bradykinin-potentiating peptide Cdt1b; Bradykinin-potentiating peptide Cdt2; Bradykinin inhibitor peptide Cdt3; C-type natriuretic peptide CNP |
| Gene Name | |
| Organism | Crotalus durissus terrificus (South American rattlesnake) |
| 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) Crotalus Crotalus durissus (tropical rattlesnake) Crotalus durissus terrificus (South American rattlesnake) |
| Enzyme Sequence | MFVSRLAASGLLLLALLAVSLDGKPLQQWSQRWPHLEIPPLVVQNWKSPTQLQARESPAGGTTALREELSLGPEAALDTPPAGPDGGPRGSKAAAAAPQRLSKSKGASATSAASRDLRTDGKQARQNWGRLVSPDHHSAAGGGCGGGGGARRLKGLAKKRAGNGCFGLKLDRIGSMSGLGC |
| Enzyme Length | 181 |
| Uniprot Accession Number | Q90Y12 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Bradykinin-potentiating 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. Synthetic Cdt1a, Cdt1b and the short hexapeptide Cdt3 are able to potentiate the hypotensive effect mediated by Bk on the blood pressure of anesthetized rats. {ECO:0000269|PubMed:17714693}.; FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Compositional bias (1); Disulfide bond (1); Modified residue (4); Natural variant (3); Peptide (5); Propeptide (4); Region (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Vasoactive;Vasodilator |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15912471}. |
| Modified Residue | MOD_RES 28; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250; MOD_RES 31; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:15912471; MOD_RES 44; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250; MOD_RES 53; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,560 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |