Detail Information for IndEnz0002013096
IED ID IndEnz0002013096
Enzyme Type ID protease013096
Protein Name Thrombin-like enzyme okinaxobin-1
SVTLE
EC 3.4.21.-
Fibrinogen-clotting enzyme
Okinaxobin I
Snake venom serine protease
SVSP
Fragment
Gene Name
Organism Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis)
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) Ovophis Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis)
Enzyme Sequence VIGGDECNINEHRFLAALYD
Enzyme Length 20
Uniprot Accession Number P20005
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Strongly inactivated by diisopropylfluorophosphate (DFP) and phenylmethanesulfonyl fluoride (PMSF), and to a lesser extent by tosyl-L-lysine chloromethyl ketone (TLCK). {ECO:0000269|PubMed:1964457}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Thrombin-like snake venom serine protease that releases specifically fibrinopeptide B from fibrinogen (FGB) to form fibrin clots. Shows a preferential cleavage at Arg-|-Gly bonds in fibrinogen beta chains. Cleaves fibrinogen beta chains preferentially to alpha chains. {ECO:0000269|PubMed:1964457, ECO:0000269|PubMed:7725319}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Non-terminal residue (1)
Keywords Blood coagulation cascade activating toxin;Direct protein sequencing;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1964457}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:1964457}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 2,249
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=73 uM for tosyl-L-arginine methyl ester (TAME) {ECO:0000269|PubMed:7725319}; KM=40 uM for benzoyl-L-arginine p-nitroanilide (BAPA) {ECO:0000269|PubMed:7725319};
Metal Binding
Rhea ID
Cross Reference Brenda