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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
-
-
?