Detail Information for IndEnz0002009950
IED ID IndEnz0002009950
Enzyme Type ID protease009950
Protein Name Serine protease harobin
EC 3.4.21.-
Fibrin
ogen
olytic enzyme
Snake venom serine protease
SVSP
Gene Name
Organism Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis hardwickii)
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 Hydrophiidae Hydrophis Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis hardwickii)
Enzyme Sequence MPLIRVLASLLILQLSYGKSLDNGAKAITSLDRIIGGFECNPSEHRSLVYLYNSAGFFCSGTLLNHEWVLTAAHCNREDIQIRLGVHNVHVHYEDEQIRVPKEKLCCLSTNNCTQFSQDIMLIRLNSPVNYSEHIAPLSLPSNPPSMGSVCCVMGWGTITSPEVTYPEVPHCVDINILHIPVCQAAYPTMSGKNILCAGILEGGKDSCKGDSGGPLICNGQIQGIVSWGRFPCAQFLEPGIYTKVFDYKDWIEGIIAGNSNVICP
Enzyme Length 265
Uniprot Accession Number Q5MCS0
Absorption
Active Site ACT_SITE 74; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 119; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 212; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:17544404}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Serine protein with fibrinolytic and fibrinogenolytic activities. Degrades Bbeta-chain (FGB) of fibrinogen first and then the Aalpha-chain (FGA). Gamma-chain (FGG) are also digested on prolonged incubation. In vitro, it cleaves high molecular weight (HMW) kininogen (KNG) releasing bradykinin that promotes vasodilation. In vitro and in vivo, it cleaves angiotensin-2 (AGT). This explains the reduction of blood pressure in hypertensive rats. Has also antithrombotic effects on thrombosis animal models. {ECO:0000269|PubMed:17544404}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:17544404};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:17544404};
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (2); Mutagenesis (2); Propeptide (1); Signal peptide (1)
Keywords Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Hypotensive agent;Protease;Secreted;Serine protease;Signal;Toxin;Vasoactive;Vasodilator;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Harobin contains three additional Cys residues than other snake venom serine proteases, suggesting an additional disulfide bond. In addition, it is more stable than other snake 6-disulfide-bond serine proteases, since it is less sensitive to DTT.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 28,996
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for n-p-tosyl-gly-pro-arg p-nitroanilide {ECO:0000269|PubMed:17544404};
Metal Binding
Rhea ID
Cross Reference Brenda