3.4.21.74: venombin A
This is an abbreviated version!
For detailed information about venombin A, go to the full flat file.
Word Map on EC 3.4.21.74
-
3.4.21.74
-
clot
-
coagulation
-
timp-1
-
platelet
-
collagen
-
heparin
-
anticoagulant
-
fibrinopeptide
-
metalloproteinases
-
bleeding
-
thrombosis
-
plasminogen
-
mmp-9
-
prothrombin
-
thromboplastin
-
defibrinogenation
-
fibrinolysis
-
antithrombin
-
defibrination
-
dysfibrinogenemias
-
plasmin
-
hemostat
-
fibrinogenolytic
-
thrombolytic
-
rhodostoma
-
contortrix
-
trimeresurus
-
hirudin
-
malayan
-
amidolytic
-
clauss
-
copperhead
-
clottable
-
flavoviridis
-
hypofibrinogenemia
-
rattlesnake
-
heparin-induced
-
moojeni
-
antivenoms
-
aalpha
-
jararaca
-
acutus
-
halys
-
protac
-
euglobulin
-
analysis
-
medicine
-
piiinp
-
2-antiplasmin
-
kallikrein-like
-
pharmacology
-
protofibrils
-
viperidae
-
drug development
- 3.4.21.74
- clot
- coagulation
- timp-1
- platelet
- collagen
- heparin
-
anticoagulant
-
fibrinopeptide
- metalloproteinases
- bleeding
- thrombosis
- plasminogen
- mmp-9
- prothrombin
- thromboplastin
-
defibrinogenation
-
fibrinolysis
- antithrombin
-
defibrination
-
dysfibrinogenemias
- plasmin
-
hemostat
-
fibrinogenolytic
-
thrombolytic
- rhodostoma
- contortrix
- trimeresurus
- hirudin
-
malayan
-
amidolytic
-
clauss
- copperhead
-
clottable
- flavoviridis
- hypofibrinogenemia
- rattlesnake
-
heparin-induced
- moojeni
- antivenoms
-
aalpha
- jararaca
- acutus
- halys
- protac
-
euglobulin
- analysis
- medicine
-
piiinp
-
2-antiplasmin
-
kallikrein-like
- pharmacology
-
protofibrils
- viperidae
- drug development
Reaction
Selective cleavage of Arg-/- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme =
Synonyms
AaV-SP-II, albofibrase1, alpha fibrinogenase, alpha-Fibrinogenase, Ancrod, Batroxobin, beta-fibrinogenase, Bhalternin, bothrombin, Bothrops atrox serine proteinase, BpirSP-39, coagulant serine protease, Crotalase, Dav-PA, EC 3.4.21.28, EC 3.4.21.29, EC 3.4.21.30, gloshedobin, Habutobin, Lachesis stenophrys venom serine proteinase, metalloproteinase 1, Mutase, acetolactate, Protein C activator, Reptilase, Russell's viper basic coagulant metalloprotease, RVBCMP, RVV protease, snake venom serine protease, TA-2, Thrombin-like enzyme, thrombin-like serine protease, TLE, Vaa serine proteinase homolog 1, VaaSPH-1, VaF1, venom gloshedobin, viper venom serine protease, VLAF, VLBF, VLCII
ECTree
3.4.21.74 venombin AAdvanced search results
results (
results (General Information
General Information on EC 3.4.21.74 - venombin A
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the peptidase S1 family, snake venom subfamily
metabolism
physiological function
additional information
metabolism
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
metabolism
Macrovipera lebetina cernovi
-
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
metabolism
Macrovipera lebetina lebetina
-
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
metabolism
-
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
metabolism
-
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
physiological function
-
the enzyme causes morphological alterations in heart, liver, lung and muscle of mice and causes blood clotting in vitro and defibrinogenation when intraperitoneally administered to mice, suggesting it to be a thrombin-like enzyme
physiological function
-
the enzyme acts as a promoter for platelet aggregation induced by ADP or collagen. It causes prolongation of bleeding in mice, but has no hemorrhagic and edema-inducing activities even at high concentrations
physiological function
-
the enzyme is able to form fibrin networks. It promotes platelet aggregation and also exhibits fibrinogenolytic, fibrinolytic, gelatinolytic, and amidolytic activities
physiological function
a glycoprotein from the nose-horned viper (Vipera ammodytes ammodytes [Vaa]) venom, Vaa serine proteinase homolog 1 (VaaSPH-1), structurally is a serine protease but without an enzymatic activity. It exhibits potent anticoagulant action in human blood. One of its targets in the blood coagulation system is FVIIIa of the intrinsic tenase complex, where VaaSPH-1 antagonizes the binding of FIXa. VaaSPH-1 also inhibits extrinsic tenase activity
physiological function
enzyme VaF1 is a high molecular mass metalloproteinase with alpha-fibrinogenolytic activity from nose-horned viper (Vipera ammodytes ammodytes) venom
physiological function
the enzyme degrades the fibrinogen alpha-chain. VLAF is active on casein but not on esters and amides of arginine. It splits the oxidized insulin B-chain at Tyr16-Leu17, Phe24-Phe25 and Phe25-Tyr26, and glucagon at Tyr10-Ser11, Leu14-Asp15 and Leu26-Met27. Alpha-fibrinogenase has N-terminal similarity with snake venom arginine esterases but does not hydrolyze the esters of arginine, lysine and tyrosine. The enzyme has strong proteolytic activity and degrades the alpha-chain of fibrinogen altering its clottability by thrombin
physiological function
VLBF cleaves in fibrinogen the Bbeta-chain first and later also the Aalpha-chain. VLBF is a glycoprotein containing 23% of neutral sugars, and has extremely high thermostability. The enzyme is active on esters and amides of arginine, but not lysine esters. Beta-fibrinogenase is a typical arginine esterase, which hydrolyzes esters and amides of arginine and attacks mainly the beta-chain of fibrinogen
physiological function
Macrovipera lebetina lebetina
-
VLCII displays proaggregating effect on human platelet in a concentration-dependent manner with absence of lag time
additional information
gloshedobin is a thrombin-like enzyme from the venom of Gloydius shedaoensis
additional information
-
gloshedobin is a thrombin-like enzyme from the venom of Gloydius shedaoensis
additional information
-
the catalytic triad comprises residues His42, Asp86, and Ser194, simulation of molecular dynamics, overview
additional information
construction of a three-dimensional model of VaaSPH-1 bound to FVIIIa
additional information
determination of 13 surface-located B cell-recognized linear epitopes of a Lachesis stenophrys venom serine proteinase. The corresponding peptides are synthesized and their immunoreactivity is analyzed against a panel of experimental and therapeutic antivenoms. Molecular modeling of the Lachesis stenophrys enzyme using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D
additional information
-
determination of 13 surface-located B cell-recognized linear epitopes of a Lachesis stenophrys venom serine proteinase. The corresponding peptides are synthesized and their immunoreactivity is analyzed against a panel of experimental and therapeutic antivenoms. Molecular modeling of the Lachesis stenophrys enzyme using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D
additional information
molecular modeling of the Lachesis stenophrys enzyme (Q072L7) using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D
