| IED ID | IndEnz0002004692 |
| Enzyme Type ID | protease004692 |
| Protein Name |
Bradykinin-potentiating and C-type natriuretic peptides isoform 2 BPP-CNP Cleaved into: Bradykinin-potentiating peptide 10a BPP-10a ; Bradykinin-potentiating peptide 6a BPP-6a ; Bradykinin-potentiating peptide 13a BPP-13a Bradykinin-potentiating peptide XIIIa BPP-XIIIa ; Bradykinin-potentiating peptide 10c BPP-10c BPP-2 Bradykinin-potentiating peptide Xc BPP-Xc ; Bradykinin-potentiating peptide 10c-F BPP-10c-F ; Bradykinin-potentiating peptide 11b BPP-11b ; Bradykinin-potentiating peptide AP BPP-AP ; Bradykinin-potentiating peptide 11e BPP-11e Bradykinin-potentiating peptide XIe BPP-XIe ; Bradykinin-potentiating peptide 5a BPP-5a Bradykinin-potentiating peptide Va BPPVa Fragment |
| Gene Name | |
| Organism | Bothrops jararacussu (Jararacussu) |
| 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 jararacussu (Jararacussu) |
| Enzyme Sequence | MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPQLLVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRPPGPPIPPLTVQQWAQARPPHPPIPPAPLQKWAPVQKWAPVQKWAPVQKWAPLLQPT |
| Enzyme Length | 144 |
| Uniprot Accession Number | Q7T1M3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Bradykinin-potentiating peptide 10c]: Peptide with several activities. It inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar to that evoked by 0,5 ug of bradykinin, when injected alone into rats. It has a high bradykinin-potentiating effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 ug of bradykinin into rats (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows potent and long-lasting antihypertensive activity as well as a reduction of the heart rate (PubMed:17475904). It also binds and dose-dependently promotes the activation of cytosolic argininosuccinate synthase (ASS1), an enzyme that catalyzes the conversion of citrulline, L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It also enhances ASS1-dependent arginine production in HEK 293 cells, as well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In addition, it induces the production of nitric-oxide (NO) by HUVEC cells via the endothelial nitric-oxide synthase (NOS3), which use arginine as a substrate and produce NO. It has been shown to be internalized by ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is detected homogenously distributed within the cell cytoplasm for up to 2 hours (PubMed:19491403). {ECO:0000269|PubMed:11994001, ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403, ECO:0000269|PubMed:22869554}.; FUNCTION: [Bradykinin-potentiating peptide 11e]: Acts as indirect hypotensive agent. Increases leukocyte rolling flux and adhesion by five-fold in post-capillary venules, without any increments in vasodilation of arterioles.; FUNCTION: [Bradykinin-potentiating peptide AP]: Acts as indirect hypotensive agent. Potently induces vasodilation of arterioles, with only a small increase in leukocyte rolling flux. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Modified residue (7); Mutagenesis (5); Non-terminal residue (1); Peptide (10); Propeptide (8); Region (1); Signal peptide (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Vasoactive |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18200607, ECO:0000269|PubMed:18400032}. Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey cells. |
| Modified Residue | MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q6LEM5"; MOD_RES 48; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18200607"; MOD_RES 68; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15912471"; MOD_RES 85; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15912471"; MOD_RES 103; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18400032"; MOD_RES 117; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:P68515"; MOD_RES 123; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:P68515" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,982 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |