| IED ID | IndEnz0002013984 |
| Enzyme Type ID | protease013984 |
| Protein Name |
Bradykinin-potentiating and C-type natriuretic peptides BPP-CNP Cleaved into: Bradykinin-potentiating peptide 1 BPP 1 ; Bradykinin-potentiating peptide 2 BPP 2 ; Bradykinin-potentiating peptide 3 BPP 3 ; Bradykinin-potentiating peptide 4 BPP 4 ; Bradykinin-potentiating peptide 5 BPP 5 ; Bradykinin inhibitor peptide BIP ; C-type natriuretic peptide CNP |
| Gene Name | |
| Organism | Lachesis muta muta (Bushmaster) |
| 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) Lachesis Lachesis muta (South American bushmaster) Lachesis muta muta (Bushmaster) |
| Enzyme Sequence | MFVSRLAASGLLLLALLAVSLDGKPVQQWSHKGWPPRPQIPPLVVQQWSQKPWPPGHHIPPVVVQEWPPGHHIPPLVVQQWSQKKWPPGHHIPPLVVQKWDPPPISPPLLKPHESPAGGTTALREELSLGPEAALDTPPAGPDVGPRGSKAPAAPHRLPKSKGASATSAASRPMRDLRTDGKQARQNWGRMMNPDHHAVGGGGGGGGARRLKGLAKKRVGDGCFGLKLDRIGSMSGLGC |
| Enzyme Length | 239 |
| Uniprot Accession Number | Q27J49 |
| 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 (By similarity). {ECO:0000250}.; FUNCTION: Bradykinin inhibitor peptide antagonizes the vasodilatory actions of bradykinin at the B2 bradykinin receptor. {ECO:0000269|PubMed:16277978}.; 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 | Disulfide bond (1); Modified residue (4); Peptide (7); Propeptide (7); 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:15876444, ECO:0000269|PubMed:16277978}. |
| Modified Residue | MOD_RES 50; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:15876444; MOD_RES 65; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:15876444; MOD_RES 83; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:15876444; MOD_RES 98; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:15876444 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,453 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |