Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Albumin + H2O
?
-
bovine substrate
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
?
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
Benzoyl-Pro-Phe-Arg 4-nitroanilide + H2O
Benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Phe 4-nitrophenyl ester + H2O
benzyloxycarbonyl-Phe + 4-nitrophenol
-
-
-
?
Boc-Leu-Ser-Thr-Arg-p-nitroanilide + H2O
p-nitroaniline + Boc-Leu-Ser-Thr-Arg
-
weaker proteolytic activity than with Bz-DL-Arg-p-nitroaniline
-
-
?
Bovine fibrinogen + H2O
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bz-DL-Arg-p-nitroanilide + H2O
p-nitroaniline + Bz-DL-Arg
-
proteolytic activity
-
-
?
Carbobenzoxyl-Glu-(alpha-t-butoxy)-Gly-Arg 4-nitroanilide + H2O
Carbobenzoxyl-Glu-(alpha-t-butoxy)-Gly-Arg + 4-nitroaniline
-
-
-
?
carbobenzoxyl-Glu-(alpha-tert-butoxy)-Gly-Arg-4-nitroanilide + H2O
carbobenzoxyl-Glu-(alpha-tert-butoxy)-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Collagen IV + H2O
?
partial hydrolysis
-
-
?
D-aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide + H2O
D-aminobutyric acid-cyclohexylalanyl-Lys + 4-nitroaniline
-
-
-
?
D-Phe-L-pipecoyl-L-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
D-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
D-Val-L-Leu-L-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
factor X + H2O
?
low activity, the heavy chain of factor X is more susceptible to hydrolysis by VaF1 than the light chain whose hydrolysis is observed only after prolonged incubation, partial hydrolysis
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
fibrinogen + H2O
fibrin + fibrinopeptide B
cleavage in the beta-chain
-
-
?
Fibrinogen Aalpha-chains + H2O
?
-
-
-
-
?
fibrinogen B-beta-chain + H2O
?
-
-
-
-
?
fibrinogen-releasing peptide A + H2O
?
-
the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B
-
-
?
fibrinogen-releasing peptide B + H2O
?
-
the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B
-
-
?
Fibronectin + H2O
?
partial hydrolysis
-
-
?
Gelatin + H2O
?
-
degradation
-
-
?
H-D-Cyclohexylglycyl-aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-aminobutyric acid-cyclohexylalanyl-Lys + 4-nitroaniline
-
-
-
?
H-D-Cyclohexylglycyl-L-2-aminobutyryl-Arg 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-L-alpha-aminobutyryl-L-arginine + 4-nitroaniline
-
-
-
-
?
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide + H2O
H-D-Hexahydrotyrosyl-Ala-Arg + 4-nitroaniline
-
-
-
?
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide + H2O
H-D-Nle-cyclohexylalanyl-L-arginine + 4-nitroaniline
-
-
-
?
H-D-Nle-hexahydrotyrosyl-Lys 4-nitroanilide + H2O
H-D-Nle-hexahydrotyrosyl-Lys + 4-nitroaniline
-
-
-
?
H-D-Phenylglycyl-Phe-Arg 4-nitroanilide + H2O
H-D-Phenylglycyl-Phe-Arg + 4-nitroaniline
-
-
-
?
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide + H2O
H-D-Pro-hexahydrotyrosyl-L-arginine + 4-nitroaniline
-
-
-
?
Human blood coagulation factor XIII + H2O
Activated human blood coagulation factor XIII
human plasma fibrinogen + H2O
?
-
the fibrinogen degradation products are separated by RP-HPLC followed by mass spectrometric analysis
-
-
?
Insulin B-chain + H2O
?
-
-
-
?
Methylsulfonyl-Leu-Gly-Arg 4-nitroanilide + H2O
Methylsulfonyl-Leu-Gly-Arg + 4-nitroaniline
-
-
-
?
N-benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide + H2O
N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginyl 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
amidolytic activity
-
-
?
Nalpha-Benzoyl-L-Arg cyclohexyl ester + H2O
Nalpha-Benzoyl-L-Arg + cyclohexanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
Nalpha-Benzoyl-L-Arg methyl ester + H2O
Nalpha-Benzoyl-L-Arg + methanol
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-arginine-4-nitroanilide + H2O
Nalpha-benzyloxycarbonyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
Nalpha-tosyl-Gly-Pro-Arg + 4-nitrolaniline
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage sites: Tyr16-Leu17 (isozymes A1-3), Gly23-Phe24, Phe25-Val26 (isozymes A1 and 2), His5-Leu6 (isozyme A1), His10-Leu11, Leu15-Tyr16, Phe24-Phe25 (isozyme A2)
-
?
plasminogen + H2O
?
low activity, partial hydrolysis
-
-
?
prothrombin + H2O
?
low activity, partial hydrolysis
-
-
?
S-2222 + H2O
?
-
chromogenic substrate
-
-
?
Tosyl-Gly-Pro-Arg 4-nitroanilide + H2O
Tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
Tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
additional information
?
-
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
Bovine fibrinogen + H2O
?
-
the fibrinogen degradation products are separated by RP-HPLC followed by mass spectrometric analysis
-
-
?
Bovine fibrinogen + H2O
?
-
coagulation
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
high activity
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
-
-
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
-
-
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
-
-
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
-
-
-
-
?
factor XIII + H2O
?
-
activation
-
-
?
factor XIII + H2O
?
-
activation of the factor in the blood coagulation cascade
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
bovine substrate, the enzyme cleaves preferentially the Aalpha-chain, apparently not degrading the Bbeta and gamma-chains
-
-
?
Fibrinogen + H2O
?
-
splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain
-
-
?
Fibrinogen + H2O
?
-
human fibrinogen is a better substrate than rabbit fibrinogen
-
-
?
Fibrinogen + H2O
?
-
splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain
-
-
?
Fibrinogen + H2O
?
-
human fibrinogen is a better substrate than rabbit fibrinogen
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain
-
-
?
Fibrinogen + H2O
?
-
human fibrinogen is a better substrate than rabbit fibrinogen
-
-
?
Fibrinogen + H2O
?
-
splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain
-
-
?
Fibrinogen + H2O
?
-
human fibrinogen is a better substrate than rabbit fibrinogen
-
-
?
Fibrinogen + H2O
?
-
splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain
-
-
?
Fibrinogen + H2O
?
-
or gamma-chain
-
-
?
Fibrinogen + H2O
?
-
recombinant ancrod coagulates fibrinogen by hydrolysis of the Aalpha chain similar to the native protein
-
-
?
Fibrinogen + H2O
?
-
three of numerous fibrinogenases of Crotalus atrox venom
-
-
?
Fibrinogen + H2O
?
cleavage of the alpha-chain and the beta-chain, but not of the gamma-chain. The band of alpha chain of fibrinogen became invisible on the gel after 2 h of the reaction. Moreover, the beta chain of fibrinogen is fully digested after 24 h of the reaction
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
cleaves peptide bonds in the Aalpha-chain
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
-
acts on coagulation through both pro-and anticoagulant mechanisms
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
cleavage in the alpha-chain
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A
cleavage in the alpha-chain, low activity
-
-
?
Human blood coagulation factor XIII + H2O
Activated human blood coagulation factor XIII
-
activation, Bothrops asper and Bothrops moojeni, but not Bothrops majaroensis enzyme
-
?
Human blood coagulation factor XIII + H2O
Activated human blood coagulation factor XIII
-
activation, Bothrops asper and Bothrops moojeni, but not Bothrops majaroensis enzyme
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
-
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
-
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
-
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
-
-
-
-
?
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
-
-
-
-
?
additional information
?
-
-
no activation of plasminogen
-
-
?
additional information
?
-
-
clot formation with human plasma or bovine fibrinogen as substrate
-
-
?
additional information
?
-
-
fibrinogen beta-chain
-
-
?
additional information
?
-
-
no activation of plasminogen
-
-
?
additional information
?
-
-
clot formation with human plasma or bovine fibrinogen as substrate
-
-
?
additional information
?
-
-
fibrinogen beta-chain
-
-
?
additional information
?
-
-
no activation of human factor VIII
-
-
?
additional information
?
-
-
no activation of plasminogen
-
-
?
additional information
?
-
-
clot formation with human plasma or bovine fibrinogen as substrate
-
-
?
additional information
?
-
-
fibrinogen beta-chain
-
-
?
additional information
?
-
-
no activation of plasminogen
-
-
?
additional information
?
-
-
clot formation with human plasma or bovine fibrinogen as substrate
-
-
?
additional information
?
-
-
fibrinogen beta-chain
-
-
?
additional information
?
-
-
no activation of human factor VIII
-
-
?
additional information
?
-
-
Ancrod has a high degree of specificity for Arg esters and peptide bonds involving carboxyl group of Arg residues
-
-
?
additional information
?
-
-
no hydrolysis of native casein, denatured hemoglobin, Nalpha-benzoyl-Arg ethyl ester
-
-
?
additional information
?
-
-
does not cleave fibrinopeptide B and does not activate factor XIII
-
?
additional information
?
-
-
no plasmin-like activity
-
-
?
additional information
?
-
-
plasminogen, methoxycarbonyl-cyclohexylglycyl-Gly-Arg 4-nitroanilide
-
-
?
additional information
?
-
-
specificity compared to that of thrombin and kallikrein
-
-
?
additional information
?
-
-
hydrolyzes Arg-bonds better than Lys-bonds
-
-
?
additional information
?
-
-
fibrinogen gamma-chain
-
-
?
additional information
?
-
-
RVBCMP exerts dose-dependent coagulation of platelet-poor human plasma. RVBCMP does not show oedema induction, direct haemolysis of washed erythrocytes, hydrolysis of human plasma albumin or globulin, and thrombin-like activity, but exhibits caseinolytic, alpha-fibrinogenolytic, and liver tissue haemorrhagic activities. RVBCMP up to a dose of 25 mg/ml has no detectable phospholipase A2, acetylcholinesterase, and ATPase activities
-
-
?
additional information
?
-
-
specific activity of these protease isoenzymes against various protein substrates, overview. No activity with bovine serum globulin and azocasein
-
-
?
additional information
?
-
recombinant NusA-fusion gloshedobin shows both fibrinogen clotting and fibrinogenolytic activities
-
-
?
additional information
?
-
-
recombinant NusA-fusion gloshedobin shows both fibrinogen clotting and fibrinogenolytic activities
-
-
?
additional information
?
-
-
VLAF is inactive towards low molecular weight esters of arginine, lysine or tyrosine
-
?
additional information
?
-
the enzyme shows no esterolytic activity
-
-
?
additional information
?
-
the enzyme shows no esterolytic activity
-
-
?
additional information
?
-
-
the thrombin-like enzyme VLCII hydrolyzes the chromogenic substrate Nalpha-benzyloxycarbonyl-L-arginine-4-nitroanilide hydrochloride, but not benzoylarginine ethyl ester (BAEE). The enzyme shows high coagulant activity against human plasma and cleaved both Aalpha- and Bbeta-chain of bovine fibrinogen
-
-
?
additional information
?
-
-
no activity with Bz-Tyr-p-nitroaniline
-
-
?
additional information
?
-
-
no activity with fibrin, but high esterase activity with Nalpha-4-tosyl-L-arginine methyl ester
-
-
?
additional information
?
-
binding of enzyme VaaSPH-1 to lipids, overview
-
-
?
additional information
?
-
enzyme VaF1 degrades collagen IV, nidogen and fibronectin, components of the extracellular matrix in vitro, although with low efficacy and narrow specificity. Although VaF1 possesses a collagen-binding sequence in its disintegrin-like domain, VaF1 displays no effect on collagen-induced platelet aggregation in vitro. The two major coagulation factors, FX and prothrombin, and the fibrinolysis factor, plasminogen, are only partially hydrolysed by VaF1 in vitro. FX and plasminogen are degraded also very slowly. None of the degradation products detected by SDS-PAGE analysis has the same apparent molecular mass as the heavy chains of the activated factors, FXa, alpha-thrombin and plasmin, overview. No activity with laminin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-Nitrophenyl-4-guanidinobenzoate
-
-
Alpha-macroglobulin
-
-
-
alpha-N-(4-Nitrobenzyloxycarbonyl)-Arg chloromethyl ketone
-
-
diisopropyl fluorophosphate
diisopropylfluorophosphate
-
dithiothreitol
-
at 2 mM completely inhibits coagulant and protease activities of RVBCMP
EDTA
-
at 2 mM completely inhibits coagulant and protease activities of RVBCMP
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide
-
substrate inhibition, 1.24 mM and above
H-D-Phenylglycyl-Phe-Arg 4-nitroanilide
-
substrate inhibition, 0.31 mM and above
N-tosyl-L-phenylalanine chloromethyl ketone
strong inhibition
phenylmethylsulfonyl fluoride
strong inhibition
polyvalent antivenom
-
inhibits the coagulant, protease, and haemorrhagic activities of RVBCMP in a dose-dependent manner, but to a different extent
-
Pro-Phe-Arg chloromethyl ketone
-
kinetics
Soybean trypsin inhibitor
-
diisopropyl fluorophosphate
-
2.5 mM, pH 8
diisopropyl fluorophosphate
-
2.5 mM, pH 8
diisopropyl fluorophosphate
-
2.5 mM, pH 8
diisopropyl fluorophosphate
-
2.5 mM, pH 8
diisopropyl fluorophosphate
-
-
PMSF
-
-
Soybean trypsin inhibitor
-
not
-
Soybean trypsin inhibitor
-
not
-
Soybean trypsin inhibitor
-
not
-
Soybean trypsin inhibitor
-
not
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
partial inhibition
-
additional information
-
no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
-
additional information
-
no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
-
additional information
-
fibrinogenolytic activity is completely inhibited by metalloprotease inhibitors
-
additional information
-
no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
-
additional information
-
no inhibition by SDS, iodoacetamide, heparin, heparinoids, hirudin, aprotinin, epsilon-aminocaproic acid, tranexamic acid
-
additional information
-
no inhibition by Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
additional information
-
no inhibition by EDTA, 2-mercaptoethanol
-
additional information
-
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
-
additional information
no inhibition by ethylenediaminetetraacetic acid, heparin, and hirudin. 10 mM 2-mercaptoethanol and DTT have poor effects on the recombinant enzyme activity
-
additional information
-
no inhibition by ethylenediaminetetraacetic acid, heparin, and hirudin. 10 mM 2-mercaptoethanol and DTT have poor effects on the recombinant enzyme activity
-
additional information
no inhibition by EDTA
-
additional information
no inhibition by EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
the enzyme belongs to the peptidase S1 family, snake venom subfamily
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
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
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
-
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 enzyme is a thrombin-like serine protease
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15000
-
1 * 15000, SDS-PAGE, after reduction with beta-mercaptoethanol. 1 * 21000, SDS-PAGE, in the absence of reducing agent and heating
15090
-
MALDI-TOF-mass spectrometry
21000
-
1 * 15000, SDS-PAGE, after reduction with beta-mercaptoethanol. 1 * 21000, SDS-PAGE, in the absence of reducing agent and heating
23000
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
27000
-
1 * 27000, SDS-PAGE
27800
-
sequence analysis
28000
-
1 * 28000, SDS-PAGE, Autographa californica nuclear polyhedrosis virus-r-habutobin
30000 - 35000
-
Crotalus atrox, gel filtration
32901
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
33000
-
1 * 33000, Crotalus atrox, isozymes A1 and A3, SDS-PAGE
333571
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
33363
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
35000
-
1 * 35000, Crotalus atrox, isozyme A2, SDS-PAGE
35400
-
Agkistrodon rhodostoma, sedimentation equilibrium
38000
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
39000
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
39408
-
x * 39408, mass spectrometry, x * 49000, SDS-PAGE
43000
-
Bothrops marajoensis, ultracentrifugation
47900
-
1 * 47900, SDS-PAGE
49000
-
x * 39408, mass spectrometry, x * 49000, SDS-PAGE
90000
x * 90000, recombinant HusA-fusion gloshedobin, SDS-PAGE
30000
-
-
30000
-
x * 30000, SDS-PAGE, recombinant active enzyme including 2.2 kDa of glycosylation
31100
-
-
32000
-
1 * 32000, Bothrops asper, SDS-PAGE
32000
-
1 * 32000, Bothrops asper, SDS-PAGE
32000
-
1 * 32000, Bothrops asper, SDS-PAGE
36000
-
1 * 36000, Bothrops moojeni, SDS-PAGE
36000
-
1 * 36000, Bothrops moojeni, SDS-PAGE
36000
-
1 * 36000, Bothrops moojeni, SDS-PAGE
37000
-
Bothrops moojeni, ultracentrifugation
37000
-
1 * 37000, SDS-PAGE
41500
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
41500
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
41500
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
additional information
-
amino acid composition
additional information
-
amino acid sequence homology between crotolase, bovine thrombin and porcine pancreatic kallikrein
additional information
-
N-terminal sequence
additional information
-
broad 43000-48000 band, corresponding to the complex glycosylated ancrod, purified protein, zymography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 39408, mass spectrometry, x * 49000, SDS-PAGE
?
-
x * 23000, about , deglycosylated isozymes, SDS-PAGE, x * 38000, isozyme RV-FVPalpha, SDS-PAGE, x * 39000, isozyme RV-FVPbeta and isozyme RV-FVPgamma, SDS-PAGE, x* 40000, isozyme RV-FVPdelta, SDS-PAGE, x * 32901, isozyme RV-FVPalpha, mass spectrometry, x * 33363, isozyme RV-FVPbeta, mass spectrometry, x * 333571, isozyme RV-FVPgamma, mass spectrometry, x* 34594, isozyme RV-FVPdelta, mass spectrometry
?
x * 90000, recombinant HusA-fusion gloshedobin, SDS-PAGE
?
-
x * 30000, SDS-PAGE, recombinant active enzyme including 2.2 kDa of glycosylation
?
x * 49700, about, mass spectrometry
monomer
-
1 * 27000, SDS-PAGE
monomer
-
1 * 32000, Bothrops asper, SDS-PAGE
monomer
-
1 * 36000, Bothrops moojeni, SDS-PAGE
monomer
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
monomer
-
1 * 32000, Bothrops asper, SDS-PAGE
monomer
-
1 * 36000, Bothrops moojeni, SDS-PAGE
monomer
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
monomer
-
1 * 32000, Bothrops asper, SDS-PAGE
monomer
-
1 * 36000, Bothrops moojeni, SDS-PAGE
monomer
-
1 * 41500, Bothrops marajoensis, SDS-PAGE
monomer
-
1 * 33000, Crotalus atrox, isozymes A1 and A3, SDS-PAGE
monomer
-
1 * 35000, Crotalus atrox, isozyme A2, SDS-PAGE
monomer
-
1 * 15000, SDS-PAGE, after reduction with beta-mercaptoethanol. 1 * 21000, SDS-PAGE, in the absence of reducing agent and heating
monomer
-
1 * 37000, SDS-PAGE
monomer
-
1 * 28000, SDS-PAGE, Autographa californica nuclear polyhedrosis virus-r-habutobin
monomer
-
1 * 47900, SDS-PAGE
additional information
-
the N-terminal sequenceis VVGGDECNIN
additional information
the typical P-IIIa subclass snake venom metalloproteinase VaF1 is composed of metalloproteinase domain, disintegrin-like domain, and cysteine-rich domain. Enzyme protein Edman sequencing and mass spectrometry
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Simmons, G.; Bundalian, M.; Theodor, I.; Martinoli, J.; Pirkle, H.
Action of crotalase, an enzyme with thrombin-like and kallikrein-like specificities, on tripeptide nitroanilide derivatives
Thromb. Res.
40
555-561
1985
Crotalus adamanteus
brenda
Markland, F.S.; Kettner, C.; Schiffman, S.; Shaw, E.; Bajwa, S.S.; Reddy, K.N.N.; Kirakossian, H.; Patkos, G.B.; Theodor, I.; Pirkle, H.
Kallikrein-like activity of crotalase, a snake venom enzyme that clots fibrinogen
Proc. Natl. Acad. Sci. USA
79
1688-1692
1982
Crotalus adamanteus
brenda
Hung, C.C.; Chiou, S.H.
Isolation of multiple isoforms of alpha-fibrinogenase from the Western diamondback rattlesnake, Crotalus atrox: N-terminal sequence homology with ancrod, an antithrombotic agent from Malayan viper
Biochem. Biophys. Res. Commun.
201
1414-1423
1994
Crotalus atrox
brenda
Itoh, N.; Tanaka, N.; Funakoshi, I.; Kawasaki, T.; Mihashi, S.; Yamashina, I.
Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family
J. Biol. Chem.
263
7628-7631
1988
Bothrops atrox, Bothrops moojeni
brenda
Stocker, K.; Barlow, G.H.
The coagulant enzyme from Bothrops atrox venom (batroxobin)
Methods Enzymol.
45
214-223
1976
Bothrops asper, Bothrops atrox, Bothrops marajoensis, Bothrops moojeni
brenda
Nakamura, M.; Kinjoh, K.; Kosugi, T.
Production of a monoclonal antibody against the thrombin-like enzyme, habutobin, from Trimeresurus flavoviridis venom
Toxicon
30
1177-1188
1992
Protobothrops flavoviridis
brenda
Nolan, C.; Hall, L.S.; Barlow, G.H.
Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
Methods Enzymol.
45
205-213
1976
Calloselasma rhodostoma
brenda
Watanabe, L.; Vieira, D.F.; Bortoleto, R.K.; Arni, R.K.
Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca
Acta Crystallogr. Sect. D
58
1036-1038
2002
Bothrops jararaca
brenda
Dempfle, C.E.; Argiriou, S.; Kucher, K.; Muller-Peltzer, H.; Rubsamen, K.; Heene, D.L.
Analysis of fibrin formation and proteolysis during intravenous administration of ancrod
Blood
96
2793-2802
2000
Calloselasma rhodostoma
brenda
Siigur, J.; Aaspollu, A.; Tonismaegi, K.; Trummal, K.; Samel, M.; Vija, H.; Subbi, J.; Siigur, E.
Proteases from Vipera lebetina Venom Affecting Coagulation and Fibrinolysis
Haemostasis
31
123-132
2001
Macrovipera lebetina
brenda
Siigur, E.; Aaspollu, A.; Siigur, J.
Anticoagulant serine fibrinogenases from Vipera lebetina venom: Structure-function relationships
Thromb. Haemost.
89
826-831
2003
Macrovipera lebetina
brenda
Sunagawa, M.; Nakamura, M.; Kosugi, T.
Cloning of habutobin cDNA and antithrombotic activity of recombinant protein
Biochem. Biophys. Res. Commun.
362
899-904
2007
Protobothrops flavoviridis
brenda
Giron, M.E.; Salazar, A.M.; Aguilar, I.; Perez, J.C.; Sanchez, E.E.; Arocha-Pinango, C.L.; Rodriguez-Acosta, A.; Guerrero, B.
Hemorrhagic, coagulant and fibrino(geno)lytic activities of crude venom and fractions from mapanare (Bothrops colombiensis) snakes
Comp. Biochem. Physiol. C
147C
113-121
2008
Bothrops colombiensis
brenda
Yu, X.; Li, Z.; Xia, X.; Fang, H.; Zhou, C.; Chen, H.
Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris
Protein Expr. Purif.
55
257-261
2007
Calloselasma rhodostoma
brenda
Muanpasitporn, C.; Rojnuckarin, P.
Expression and characterization of a recombinant fibrinogenolytic serine protease from green pit viper (Trimeresurus albolabris) venom
Toxicon
49
1083-1089
2007
Trimeresurus albolabris
brenda
Levy, D.E.; Trammel, J.; Wasiewski, W.W.; Wasiewski, W.W.
Ancrod for acute ischemic stroke: a new dosing regimen derived from analysis of prior ancrod stroke studies
J. Stroke Cerebrovasc. Dis.
18
23-27
2009
synthetic construct
brenda
Mukherjee, A.K.
Characterization of a novel pro-coagulant metalloprotease (RVBCMP) possessing alpha-fibrinogenase and tissue haemorrhagic activity from venom of Daboia russelli russelli (Russells viper): evidence of distinct coagulant and haemorrhagic sites in RVBCMP
Toxicon
51
923-933
2008
Daboia russelii russelii
brenda
Jiang, X.; Xu, J.; Yang, Q.
Soluble expression, purification, and characterization of Gloydius shedaoensis venom gloshedobin in Escherichia coli by using fusion partners
Appl. Microbiol. Biotechnol.
85
635-642
2010
Gloydius shedaoensis (P0C5B4), Gloydius shedaoensis
brenda
Costa, J.; Fonseca, K.; Neves Mamede, C.; Beletti, M.; Santos-Filho, N.; Soares, A.; Arantes, E.; Hirayama, S.; Selistre-de-Araujo, H.; Fonseca, F.; Henrique-Silva, F.; Penha-Silva, N.; Oliveira, F.
Bhalternin: Functional and structural characterization of a new thrombin-like enzyme from Bothrops alternatus snake venom
Toxicon
55
1365-1377
2010
Bothrops alternatus
brenda
Zaqueo, K.D.; Kayano, A.M.; Simoes-Silva, R.; Moreira-Dill, L.S.; Fernandes, C.F.; Fuly, A.L.; Maltarollo, V.G.; Honorio, K.M.; da Silva, S.L.; Acosta, G.; Caballol, M.A.; de Oliveira, E.; Albericio, F.; Calderon, L.A.; Soares, A.M.; Stabeli, R.G.
Isolation and biochemical characterization of a new thrombin-like serine protease from Bothrops pirajai snake venom
BioMed Res. Int.
2014
595186
2014
Bothrops pirajai
brenda
He, Q.; Li, H.; Zhou, B.; Wen, H.; Li, J.; Xiao, B.; Zhang, K.; Hodgson, W.C.; Yu, X.
TA-2, a thrombin-like enzyme from the Chinese white-lipped green pitviper (Trimeresurus albolabris): isolation, biochemical and biological characterization
Blood Coagul. Fibrinolysis
23
445-453
2012
Trimeresurus albolabris
brenda
Mukherjee, A.K.
The pro-coagulant fibrinogenolytic serine protease isoenzymes purified from Daboia russelii russelii venom coagulate the blood through factor V activation: role of glycosylation on enzymatic activity
PLoS ONE
9
e86823
2014
Daboia russelii russelii
brenda
Leonardi, A.; Sajevic, T.; Latinovic, Z.; Pungercar, J.; Lang Balija, M.; Trampus Bakija, A.; Vidmar, R.; Halassy, B.; Krizaj, I.
Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom
Biochimie
109
78-87
2015
Vipera ammodytes ammodytes (A0A0B4U9L8)
brenda
Eickhoff, R.M.; Kroh, A.; Ruebsamen, K.; Heise, D.; Binneboesel, M.; Klinge, U.; Neumann, U.P.; Klink, C.D.
AK03, a new recombinant fibrinogenase prevents abdominal adhesions in a rat model without systemic side effects
J. Surg. Res.
222
85-92
2018
Calloselasma rhodostoma (P26324)
brenda
Latinovic, Z.; Leonardi, A.; Kovacic, L.; Koh, C.; Sribar, J.; Bakija, A.; Venkateswarlu, D.; Kini, R.; Krizaj, I.
The first intrinsic tenase complex inhibitor with serine protease structure offers a new perspective in anticoagulant therapy
Thromb. Haemost.
118
1713-1728
2018
Vipera ammodytes ammodytes (A0A1I9KNP0)
brenda
Madrigal, M.; Alape-Giron, A.; Barboza-Arguedas, E.; Aguilar-Ulloa, W.; Flores-Dixadaz, M.
Identification of B cell recognized linear epitopes in a snake venom serine proteinase from the central American bushmaster Lachesis stenophrys
Toxicon
140
72-82
2017
Lachesis stenophrys (Q072L7), Lachesis stenophrys, Deinagkistrodon acutus (Q9I8X1)
brenda
Siigur, J.; Aaspollu, A.; Siigur, E.
Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies
Toxicon
158
16-32
2019
Macrovipera lebetina transmediterranea, Macrovipera lebetina cernovi, Macrovipera lebetina lebetina, Macrovipera lebetina obtusa, Macrovipera lebetina (E0Y419), Macrovipera lebetina (Q8JH85)
brenda