Information on EC 3.4.21.74 - venombin A

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.74
-
RECOMMENDED NAME
GeneOntology No.
venombin A
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
146240-35-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bothrops atrox variety
-
-
Manually annotated by BRENDA team
South American pit viper, formerly EC 3.4.21.29, different varieties
-
-
Manually annotated by BRENDA team
snakes from Caucagua and El Guapo towns of the Venezuelan state of Miranda
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bothrops atrox variety
-
-
Manually annotated by BRENDA team
from Brasil
-
-
Manually annotated by BRENDA team
Eastern diamondback rattlesnake, formerly EC 3.4.21.30
-
-
Manually annotated by BRENDA team
Western diamondback rattlesnake
-
-
Manually annotated by BRENDA team
Levantine viper
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Albumin + H2O
?
show the reaction diagram
-
bovine substrate
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
Benzoyl-Phe-Val-Arg 4-nitroanilide + H2O
?
show the reaction diagram
Benzoyl-Pro-Phe-Arg 4-nitroanilide + H2O
Benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
Benzyloxycarbonyl-Phe 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Phe + 4-nitrophenol
show the reaction diagram
-
-
-
-
Boc-Leu-Ser-Thr-Arg-p-nitroanilide + H2O
p-nitroaniline + Boc-Leu-Ser-Thr-Arg
show the reaction diagram
-
weaker proteolytic activity than with Bz-DL-Arg-p-nitroaniline
-
-
?
Bovine fibrinogen + H2O
?
show the reaction diagram
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
Bz-DL-Arg-p-nitroanilide + H2O
p-nitroaniline + Bz-DL-Arg
show the reaction diagram
-
proteolytic activity
-
-
?
Carbobenzoxyl-Glu-(alpha-t-butoxy)-Gly-Arg 4-nitroanilide + H2O
Carbobenzoxyl-Glu-(alpha-t-butoxy)-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
casein + H2O
?
show the reaction diagram
D-aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide + H2O
D-aminobutyric acid-cyclohexylalanyl-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
D-Phe-L-pipecoyl-L-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroanilide
show the reaction diagram
-
chromogenic substrate
-
-
?
D-Pro-L-Phe-L-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
chromogenic substrate
-
-
?
D-Val-L-Leu-L-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Dansyl-Gly-Gly-Val-Arg-Gly methyl ester + H2O
?
show the reaction diagram
factor XIII + H2O
?
show the reaction diagram
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrinopeptide A
show the reaction diagram
Fibrinogen Aalpha-chains + H2O
?
show the reaction diagram
-
-
-
-
-
fibrinogen B-beta-chain + H2O
?
show the reaction diagram
-
-
-
-
-
fibrinogen-releasing peptide A + H2O
?
show the reaction diagram
-
the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B
-
-
?
fibrinogen-releasing peptide B + H2O
?
show the reaction diagram
-
the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
degradation
-
-
?
H-D-Cyclohexylglycyl-aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-aminobutyric acid-cyclohexylalanyl-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
H-D-Cyclohexylglycyl-L-2-aminobutyryl-Arg 4-nitroanilide + H2O
H-D-Cyclohexylglycyl-L-alpha-aminobutyryl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide + H2O
H-D-Hexahydrotyrosyl-Ala-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide + H2O
H-D-Nle-cyclohexylalanyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
H-D-Nle-hexahydrotyrosyl-Lys 4-nitroanilide + H2O
H-D-Nle-hexahydrotyrosyl-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
H-D-Phenylglycyl-Phe-Arg 4-nitroanilide + H2O
H-D-Phenylglycyl-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide + H2O
H-D-Pro-hexahydrotyrosyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
Human blood coagulation factor XIII + H2O
Activated human blood coagulation factor XIII
show the reaction diagram
human plasma fibrinogen + H2O
?
show the reaction diagram
-
the fibrinogen degradation products are separated by RP-HPLC followed by mass spectrometric analysis
-
-
?
Methylsulfonyl-Leu-Gly-Arg 4-nitroanilide + H2O
Methylsulfonyl-Leu-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
N-benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide + H2O
N-benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
show the reaction diagram
-
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-DL-arginyl 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
amidolytic activity
-
-
?
Nalpha-Benzoyl-L-Arg cyclohexyl ester + H2O
Nalpha-Benzoyl-L-Arg + cyclohexanol
show the reaction diagram
-
-
-
-
-
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
show the reaction diagram
Nalpha-Benzoyl-L-Arg methyl ester + H2O
Nalpha-Benzoyl-L-Arg + methanol
show the reaction diagram
-
-
-
-
-
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-Gly-Pro-Arg-4-nitroazide + H2O
?
show the reaction diagram
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
-
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)
-
-
S-2222 + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
Tosyl-Gly-Pro-Arg 4-nitroanilide + H2O
Tosyl-Gly-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
Tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
Tosyl-L-arginine methyl ester + H2O
Tosyl-L-arginine + methanol
show the reaction diagram
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
factor XIII + H2O
?
show the reaction diagram
-
activation of the factor in the blood coagulation cascade
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrinopeptide A
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
has the highest stimulating effect of all metal ion at 2 mM, maximum coagulant activity in the presence of 7 mM Ca2+
Cu2+
-
at 2 mM 10% less active than Ca2+
Mg2+
-
at 2 mM 19% less active than Ca2+
Mn2+
-
has the least influence on RVBCMP-induced coagulation of human plasma, at 2 mM 30% less active than Ca2+
Ni2+
-
at 2 mM 12% less active than Ca2+
Zn2+
-
at 2 mM 8% less active than Ca2+
additional information
-
no activation by Ca2+; no metalloproteinase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Nitrophenyl-4-guanidinobenzoate
-
-
Alpha-macroglobulin
-
-
-
alpha-N-(4-Nitrobenzyloxycarbonyl)-Arg chloromethyl ketone
-
-
antithrombin III
-
-
-
Aprotinin
-
from bovine
benzamidine
-
-
diisopropyl fluorophosphate
dithiothreitol
-
at 2 mM completely inhibits coagulant and protease activities of RVBCMP
EDTA
-
at 2 mM completely inhibits coagulant and protease activities of RVBCMP
guanidinium ions
-
-
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
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
imidazole
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
benzoyl-Pro-Phe-Arg 4-nitroanilide
-
-
0.025
carbobenzoxyl-Glu-(alpha-tert-butoxy)-Gly-Arg 4-nitroanilide
-
-
0.18
D-Phe-L-pipecoyl-L-Arg 4-nitroanilide
0.06
D-Pro-L-Phe-L-Arg 4-nitroanilide
-
-
0.14
D-Val-L-Leu-L-Arg 4-nitroanilide
-
-
3.3
H-D-Aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide
-
methylsulfonyl-Leu-Gly-Arg 4-nitroanilide
0.45
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide
-
-
0.27
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide
-
H-D-phenylglycyl-Phe-Arg 4-nitroanilide
2.7
H-D-Nle-hexahydrotyrosyl-Lys 4-nitroanilide
-
-
0.058
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide
-
-
0.0066 - 0.0105
human plasma fibrinogen
-
0.3
Tosyl-Gly-Pro-Arg 4-nitroanilide
-
-
1.4
tosyl-Gly-Pro-Lys 4-nitroanilide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
benzoyl-Pro-Phe-Arg 4-nitroanilide
Crotalus adamanteus
-
-
0.16
carbobenzoyl-Glu-(alpha-tert-butoxy)-Gly-Arg 4-nitroanilide
Crotalus adamanteus
-
-
3.5
D-phenylglycyl-Phe-Arg 4-nitroanilide
Crotalus adamanteus
-
-
1.4
H-D-Aminobutyric acid-cyclohexylalanyl-Lys 4-nitroanilide
Crotalus adamanteus
-
-
0.68
H-D-Cyclohexylglycyl-L-2-aminobutyryl-Arg 4-nitroanilide
Crotalus adamanteus
-
-
0.95
H-D-Hexahydrotyrosyl-Ala-Arg 4-nitroanilide
Crotalus adamanteus
-
-
61
H-D-Nle-cyclohexylalanyl-Arg 4-nitroanilide
Crotalus adamanteus
-
-
6.9
H-D-Nle-hexahydrotyrosyl-Lys 4-nitroanilide
Crotalus adamanteus
-
-
4.9
H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide
Crotalus adamanteus
-
-
0.31 - 1.042
human plasma fibrinogen
-
1.3
Methylsulfonyl-Leu-Gly-Arg 4-nitroanilide
Crotalus adamanteus
-
-
11.5
Tosyl-Gly-Pro-Arg 4-nitroanilide
Crotalus adamanteus
-
-
0.7
tosyl-Gly-Pro-Lys 4-nitroanilide
Crotalus adamanteus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13
-
crude venom, equivalent of tyrosine formed per minute
33.7
-
tosyl-L-Arg methyl ester
49
-
3fold purified enzyme, equivalent of tyrosine formed per minute
108.6
-
purified native enzyme, pH 7.4, 37°C, substrate bovine fibrinogen
192.3
-
purified native enzyme, pH 7.4, 37°C, substrate casein
506
purified recombinant NusA-fusion gloshedobin, pH 8.0, 40°C
696
-
purified recombinant enzyme, specific fibrinogen clotting activity
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
recombinant NusA-fusion gloshedobin
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
activity range, recombinant NusA-fusion gloshedobin, profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
assay at
40
recombinant NusA-fusion gloshedobin
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
activity range, recombinant NusA-fusion gloshedobin, profile, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.9
-
isoelectric focusing
10.6
-
classical isoelectric point
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
nucleic acid source: venom gland
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
31500
-
native PAGE
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
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
38800
-
native PAGE
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
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
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
the N-terminal sequenceis VVGGDECNIN
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
space group P2(1)2(1)2(1), unit-cell parameters a = 94.81 A, b = 115.68 A, c = 155.97 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 9
5 - 6.8
-
several months stable at 5°C
29684
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
heating the RVBCMP at 40°C for 60 min at pH 7.4 does not influence the coagulant activity of the protein, whereas heating RVBCMP at 55°C for 20 min over a pH range from 7.0 to 8.0 results in only 42% of the original clotting activity remaining. Heating the RVBCP at 60°C results in a complete loss of coagulant activity
75
-
30 min, stable, isozyme A3
85
-
30 min, stable, isozymes A1 and 2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Stable to repeated freeze-thawing
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in dilute solution in physiological saline, pH 6, containing 0.02% gelatin and 0.3% of chlorobutol, enzyme isolated from Bothrops moojeni and Bothrops marajoensis, more than a year
5°C, pH 5-6.8, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, several forms, separable by electrophoresis and isoelectric focusing
-
Bothrops atrox variety
by gel filtration
-
by gel filtration, 3fold
-
by hydrophobic, affinity, and ion exchange chromatography
-
His-tagged recombinant habutobin fusion protein pET-r-habutobin and Autographa californica nuclear polyhedrosis virus-r-habutobin, purified by bacterial system and baculoviral system. PET-r-habutobin purified on Ni2+-NTA column
-
multiple isoforms
-
native enzyme 12.7fold from venom to homogeneity by gel filtration, anion exchange and heparin affinity chromatography
-
native enzyme from venom by anion exchange chromatography, gel filtration, and benzamidine affinity chromatography
-
native enzyme from venom by gel filtration, benzamidine affinity chromatography and reversed-phase gel filtration on a C2/C18 column
-
soluble recombinant NusA-fusion gloshedobin from Escherichia coli by hydrophobic interaction chromatograpy, two steps of anion exchange chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Bothrops atrox, moojeni
-
cDNA cloning
-
cDNA encoding ancrod synthesized with a yeast bias codon and inserted into the eukaryotic expression vector pPIC9, subsequently expressed in Pichia pastoris strain GS115
-
DNA and amino acid sequence determination and analysis
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expression of the enzyme N-terminally fused separately to three fusion partners, NusA, GST, and TrxA, expression in Escherichia coli strain BL21-Gold (DE3). NusA is the most efficient fusion partner to improve the solubility of recombinant gloshedobin, subcloning in Escherichia coli strain JM109
pET-r-habutobin expressed in inclusion body of Escherichia coli. Autographa californica nuclear polyhedrosis virus and the habutobin/pPSC12 plasmid co-transfected into Sf9 cells
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recombinant albofibrase1 expressed in Pichia pastoris strain X-33
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
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Bhaltenin may be of interest as a therapeutic agent in the treatment and prevention of thrombotic disorders