Detail Information for IndEnz0002010309
IED ID IndEnz0002010309
Enzyme Type ID protease010309
Protein Name Zinc metalloproteinase-disintegrin-like VaH1
EC 3.4.24.-
Snake venom metalloprotease
SVMP
Fragments
Gene Name
Organism Vipera ammodytes ammodytes (Western sand viper)
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 Viperinae (vipers) Vipera Vipera ammodytes (Nose-horned viper) Vipera ammodytes ammodytes (Western sand viper)
Enzyme Sequence MVTKYSSIFMSPILSNPPILYFSDCSREXYQKXLTN
Enzyme Length 36
Uniprot Accession Number P0DJ44
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA, but not inhibited by iodoacetamide, PMSF and pepstatin A. {ECO:0000269|PubMed:11602279}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Snake venom zinc metalloprotease that exhibits strong hemorrhagic activity. It also degrades alpha-chain of fibrinogen (FGA), but not the beta- and the gamma-chains. Possesses potent azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at positions Ala(14)-Leu(15), followed by Tyr(16)-Leu(17) and His(10)-Leu(11). In vivo, subcutaneous injection into mice induces strong hemorrhage. {ECO:0000269|PubMed:11602279}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:11602279};
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Domain (1); Non-adjacent residues (1); Non-terminal residue (2)
Keywords Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic 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: The N-terminus is blocked.; PTM: Glycosylated.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 4,197
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.24.B36;