Detail Information for IndEnz0002011445
IED ID IndEnz0002011445
Enzyme Type ID protease011445
Protein Name Zinc metalloproteinase-disintegrin-like daborhagin-M
EC 3.4.24.-
Snake venom metalloproteinase
SVMP
Fragment
Gene Name
Organism Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
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) Daboia Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Enzyme Sequence VATSEPNRYFNPYSYVELIITVDHS
Enzyme Length 25
Uniprot Accession Number P0DJH5
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA, EGTA and 1,10-phenanthroline. Addition of Mg(2+) or Ca(2+) increases the casein hydrolysis rate. {ECO:0000269|PubMed:18554518}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose, MHD=0.86 ug) when subcutaneously injected into mice. Has potent fibrinogenolytic activity on alpha-chain of fibrinogen (FGA). Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)-Leu(15) and Tyr(16)-Leu(17) followed by His(10)-Leu(11) and Phe(24)-Phe(25). {ECO:0000269|PubMed:18554518}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Metal binding (1); Non-terminal residue (1)
Keywords Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: N-glycosylated.; PTM: Contains 16 disulfide bonds. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 2,915
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.0 uM for NFF-2 (fluorogenic substrates with cleavage at Ala-Nva);
Metal Binding METAL 17; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda