3.4.21.55: Venombin AB
This is an abbreviated version!
For detailed information about Venombin AB, go to the full flat file.

Word Map on EC 3.4.21.55
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3.4.21.55
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snake
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fibrinogen
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envenom
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viper
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lachesis
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fibrinopeptide
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bothrops
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tsv-pa
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trimeresurus
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thrombin-like
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atrox
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antivenoms
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bushmaster
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kallikrein-like
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daboia
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tosyl-l-lysine
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russelii
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fibrinogenolytic
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viperidae
- 3.4.21.55
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snake
- fibrinogen
-
envenom
- viper
-
lachesis
-
fibrinopeptide
- bothrops
-
tsv-pa
- trimeresurus
-
thrombin-like
- atrox
- antivenoms
- bushmaster
-
kallikrein-like
-
daboia
-
tosyl-l-lysine
- russelii
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fibrinogenolytic
- viperidae
Reaction
Selective cleavage at Arg-/- bonds in fibrinogen to form fibrin and release fibrinopeptides A and B =
Synonyms
Afaacytin, Gabonase, Okinaxobin II, Proteinase, Bitis gabonica venom serine, venom serine proteinase
ECTree
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Results
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1
Substrates Products
Substrates Products on EC 3.4.21.55 - Venombin AB
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REACTION DIAGRAM
Fibrin alpha-chain + H2O
Hydrolyzed fibrin alpha-chain
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fragments of low molecular mass
?
H-D-Cyclohexylglycyl-L-2-aminobutyryl-L-arginine 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-L-alpha-aminobutyryl-L-arginine + 4-nitroaniline
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i.e. CBS 34-47, chromogenic substrate
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?
Human blood coagulation factor X + H2O
Human blood coagulation factor Xa
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enzyme appears to act as substitute for both factor VIIIa and IXa by activating factor X
i.e. EC 3.4.21.6
?
Human blood coagulation factor XIII + H2O
Activated human blood coagulation factor XIII
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activates factor XIII
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?
Tripeptide nitroanilide derivatives + H2O
Tripeptide + 4-nitroaniline
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poor substrates
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?
?
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clots fibrinogen with 45 NIH (National Institute of Health) thrombin equivalent units/mg
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-
?
Fibrinopeptide A + fibrinopeptide B + ?
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removes fibrinopeptide A and than B from fibrinogen
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-
?
Fibrinogen + H2O
Fibrinopeptide A + fibrinopeptide B + ?
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cleaves Aalpha- and Bbeta-chain, preferably Aalpha, no cleavage of gamma-chain
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?
?
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i.e. Nalpha-p-tosyl-L-arginine methyl ester
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-
?
?
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insulin, glucagon, S-peptide of ribonuclease, H-D-cyclohexylglycyl-alpha-aminobutyryl-Arg 4-nitroanilide, benzoyl-Pro-Phe-Arg 4-nitroanilide, H-D-2-aminobutyryl-cyclohexylalanyl-Lys 4-nitroanilide, H-D-Nle-hexahydrotyrosyl-Lys 4-nitroanilide, benzyloxycarbonyl-gamma (alpha-t-butoxy)glutamyl-Gly-Arg 4-nitroanilide, methoxycarbonyl-D-cyclohexylglycyl-Arg 4-nitroanilide
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-
?
additional information
?
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substrate specificity, use of an donor-acceptor detection method for the investigation of proteinase activity of selected crude venoms in a high-throughput setup, enzyme activity comparisons of different species, overview. Analysis and heatmaps of coagulation factors, inflammation-associated proteins, and collagen and integrin-derived peptides during incubation with venom. All of the substrates against which activity is observed in the inhibition experiments contain arginine residues in their sequences
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?
additional information
?
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strong arginine esterase and amidase activity on synthetic substrates
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?
additional information
?
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the enzyme from Cerastes cerastes exhibits alphabeta-fibrinogenase and alpha-fibrinase properties
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-
?
additional information
?
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no hydrolysis of fibrin gamma-chains, fibrin beta-chains or gammagamma dimer
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?
additional information
?
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releases serotonin from previously loaded platelets
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?