Information on EC 3.4.21.55 - Venombin AB

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.55
-
RECOMMENDED NAME
GeneOntology No.
Venombin AB
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Selective cleavage at Arg-/- bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
show the reaction diagram
selective cleavage at Arg- bonds in fibrinogen to form fibrin and release fibrinopeptides A and B, the term -+- depicts the point of cleavage
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
104003-74-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Gaboon viper
-
-
Manually annotated by BRENDA team
Horned viper
-
-
Manually annotated by BRENDA team
Himehabu snake
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
Fibrin alpha-chain + H2O
Hydrolyzed fibrin alpha-chain
show the reaction diagram
-
-
fragments of low molecular mass
-
Fibrinogen + H2O
?
show the reaction diagram
Fibrinogen + H2O
Fibrinopeptide A + fibrinopeptide B + ?
show the reaction diagram
H-D-Cyclohexylglycyl-L-2-aminobutyryl-L-arginine 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-L-alpha-aminobutyryl-L-arginine + 4-nitroaniline
show the reaction diagram
-
i.e. CBS 34-47, chromogenic substrate
-
-
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
H-D-phenylglycine-Phe-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Human blood coagulation factor X + H2O
Human blood coagulation factor Xa
show the reaction diagram
-
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
show the reaction diagram
-
activates factor XIII
-
-
Nalpha-benzoyl-L-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
Tosyl-Gly-Pro-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Tosyl-L-Arg methyl ester + H2O
?
show the reaction diagram
Tripeptide nitroanilide derivatives + H2O
Tripeptide + 4-nitroaniline
show the reaction diagram
-
poor substrates
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrinogen + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
required for structural cohesion of afaâcytin molecule
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzamidine
-
-
diisopropyl fluorophosphate
EGTA
-
Ca2+ does not restore
fibrinogen
-
substrate inhibition, 3 mg/ml and above
-
tosyl-L-lysine chloromethyl ketone
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide
-
-
3.4
H-D-Phenylglycine-Phe-Arg 4-nitroanilide
-
-
0.82
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide
-
-
0.13
Tosyl-Gly-Pro-Arg 4-nitroanilide
-
-
2.72
tosyl-Gly-Pro-Lys 4-nitroanilide
-
-
0.12
tosyl-L-arginine methyl ester
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide
Bitis gabonica
-
-
0.952
H-D-Phenylglycine-Phe-Arg 4-nitroanilide
Bitis gabonica
-
-
0.248
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide
Bitis gabonica
-
-
0.014
Tosyl-Gly-Pro-Arg 4-nitroanilide
Bitis gabonica
-
-
0.204
tosyl-Gly-Pro-Lys 4-nitroanilide
Bitis gabonica
-
-
12.2
tosyl-L-Arg methyl ester
Bitis gabonica
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at, tosyl-Arg-methyl ester as substrate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10200
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta, SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta, SDS-PAGE, reducing conditions
28500
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta, SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta, SDS-PAGE, reducing conditions
30600
-
1 * 30600, Bitis gabonica, SDS-PAGE, reducing and nonreducing conditions
35500
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta, SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta, SDS-PAGE, reducing conditions
38250
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta, SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta, SDS-PAGE, reducing conditions
40000
-
2 * 40000, Cerastes cerastes, alphabeta (where beta consists of two disufide linked polypeptide chains beta and beta), SDS-PAGE
40500
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta, SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta, SDS-PAGE, reducing conditions
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 40000, Cerastes cerastes, alphabeta (where beta consists of two disufide linked polypeptide chains beta and beta'), SDS-PAGE
monomer
-
1 * 30600, Bitis gabonica, SDS-PAGE, reducing and nonreducing conditions
trimer
-
1 * 40500 + 1 * 35500 + 1 * 10200, Cerastes cerastes, alphabetabeta', SDS-PAGE, reducing conditions, 1 * 38250 + 1 * 28500 + 1 * 10200, Cerastes cerastes, deglycosylated enzyme, alphabetabeta', SDS-PAGE, reducing conditions
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires Ca2+ for stability in crude venom, during purification and storage of purified enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in the presence of Ca2+, 2 years
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE