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
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3.4.21.74
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clot
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coagulation
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timp-1
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platelet
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collagen
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heparin
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anticoagulant
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fibrinopeptide
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metalloproteinases
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bleeding
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thrombosis
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plasminogen
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mmp-9
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prothrombin
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thromboplastin
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defibrinogenation
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fibrinolysis
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antithrombin
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defibrination
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dysfibrinogenemias
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plasmin
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hemostat
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fibrinogenolytic
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thrombolytic
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rhodostoma
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contortrix
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trimeresurus
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hirudin
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malayan
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amidolytic
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clauss
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copperhead
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clottable
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flavoviridis
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hypofibrinogenemia
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rattlesnake
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heparin-induced
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moojeni
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antivenoms
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aalpha
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jararaca
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acutus
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halys
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protac
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euglobulin
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analysis
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medicine
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piiinp
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2-antiplasmin
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kallikrein-like
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pharmacology
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protofibrils
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viperidae
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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 (Inhibitors
Inhibitors on EC 3.4.21.74 - venombin A
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
dithiothreitol
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at 2 mM completely inhibits coagulant and protease activities of RVBCMP
EDTA
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at 2 mM completely inhibits coagulant and protease activities of RVBCMP
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide
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substrate inhibition, 1.24 mM and above
H-D-Phenylglycyl-Phe-Arg 4-nitroanilide
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substrate inhibition, 0.31 mM and above
polyvalent antivenom
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inhibits the coagulant, protease, and haemorrhagic activities of RVBCMP in a dose-dependent manner, but to a different extent
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additional information
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no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
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additional information
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no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
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additional information
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fibrinogenolytic activity is completely inhibited by metalloprotease inhibitors
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additional information
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no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
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additional information
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no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
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additional information
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no inhibition by Nalpha-p-tosyl-L-lysine chloromethyl ketone
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additional information
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treatment of RVBCMP with serine protease inhibitors phenylmethyl suphonyl fluoride and DIFP at concentrations ranging from 0.5 to 2 mM does not affect its haemorrhagic and protease activities, and at 2 mM concentration, only a minimal (2-4%) inhibition of coagulation activity occurs. Aqueous leaf extracts from Murraya koenigii, Alostonia scholaris and Azacardica indica, except Leucus lavandulaefolia, do not inhibit the coagulant or haemorrhagic activity of RVBCMP. Leucus lavandulaefolia leaf extract significantly inhibits the liver haemorrhagic activity but not the coagulant activity of RVBCMP
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additional information
no inhibition by ethylenediaminetetraacetic acid, heparin, and hirudin. 10 mM 2-mercaptoethanol and DTT have poor effects on the recombinant enzyme activity
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additional information
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no inhibition by ethylenediaminetetraacetic acid, heparin, and hirudin. 10 mM 2-mercaptoethanol and DTT have poor effects on the recombinant enzyme activity
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