Detail Information for IndEnz0002009204
IED ID IndEnz0002009204
Enzyme Type ID protease009204
Protein Name Snake venom metalloproteinase BleucMP
SVMP
EC 3.4.24.-
Fragment
Gene Name
Organism Bothrops leucurus (Whitetail lancehead)
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 leucurus (Whitetail lancehead)
Enzyme Sequence TLTSFGEWR
Enzyme Length 9
Uniprot Accession Number P0DJJ6
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline. Not inhibited by beta-mercaptoethanol, benzamidine and aprotinin. {ECO:0000269|PubMed:21130897}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Snake venom zinc metalloprotease that has fibrino(geno)lytic activities. Hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain of fibrinogen (FGB), without affecting the gamma-chain. Preferentially hydrolyzes the beta-chain (FGB) of fibrin. In vivo, shows a low edema-inducing effect. This action may be attributed to degradation of proteins in the cell membrane and consequent release of inflammatory mediators and leukocyte infiltrate. {ECO:0000269|PubMed:21130897}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (2)
Keywords Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: Contains 7 disulfide bonds.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 1,096
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda