Information on EC 3.1.15.1 - venom exonuclease

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.15.1
-
RECOMMENDED NAME
GeneOntology No.
venom exonuclease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates
show the reaction diagram
preference for single-stranded substrate
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-82-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
Bothrops pradoi
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
banded krait
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
Russell's viper
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
Gloydius halys ussuriensis
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
Formosan habu
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
snake
commercial preparation, Sigma P 4631
-
-
Manually annotated by BRENDA team
green habu
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
overview of occurrence of phosphodiesterase in venom
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the phosphodiesterase TS-PDE strongly inhibits ADP-induced platelet aggregation in human plateletrich plasma by hydrolyzing ADP
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
4-nitrophenyl thymidine-5'-phosphate + H2O
4-nitrophenol + thymidine-5'-phosphate
show the reaction diagram
5'-(dCTTCA-(2'-azetidine)T-TTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
azetidine-T modified antisense oligonucleotide 11 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCA-(2'-N-4'-C-ethylene-bridged)T-TTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
2'-N,4'-C-ethylene-bridged nucleic acid thymidine modified antisense oligonucleotide 5 still remains undegraded to certain extent
-
-
?
5'-(dCTTCA-(2'-O-(2-methoxy)ethyl)T-TTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
for 2'-O-methyl-T modified antisense oligonucleotide 7 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCA-(2'-O-methyl)T-TTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
for 2'-O-methyl-T modified antisense oligonucleotide 6 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCA-(2'-oxetane)T-TTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
-
-
-
?
5'-(dCTTCATT-(2'-azetidine)T-TTTCTTC)-3' + H2O
?
show the reaction diagram
-
azetidine-T modified antisense oligonucleotide 10 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCATT-(2'-N-4'-C-ethylene-bridged)T-TTTCTTC)-3' + H2O
?
show the reaction diagram
-
2'-N,4'-C-ethylene-bridged nucleic acid thymidine modified antisense oligonucleotide 4 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTT-(2'-azetidine)T-TCTTC)-3' + H2O
?
show the reaction diagram
-
azetidine-T modified antisense oligonucleotide 8 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCATTTT-(2'-N-4'-C-ethylene-bridged)T-TCTTC)-3' + H2O
?
show the reaction diagram
-
2'-N,4'-C-ethylene-bridged nucleic acid thymidine modified antisense oligonucleotide 3 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTTTTC-(2'-azetidine)T-TC)-3' + H2O
?
show the reaction diagram
-
azetidine-T modified antisense oligonucleotide 8 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTTTTC-(2'-N-4'-C-ethylene-bridged)T-TC)-3' + H2O
?
show the reaction diagram
-
2'-N,4'-C-ethylene-bridged nucleic acid thymidine modified antisense oligonucleotide 2 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTTTTCTTC)-3' + H2O
?
show the reaction diagram
-
unmodified antisense oligonucleotide 1 is completely degraded after 30 min
-
-
?
adenosine 5'-monophosphate-O-ethyl ester + H2O
adenosine 5'-monophosphate + ethanol
show the reaction diagram
-
-
-
ir
adenosine 5'-O-phosphorothioate-O-p-nitrophenyl ester + H2O
adenosine-5'-O-phosphorothioate + p-nitrophenol
show the reaction diagram
adenosine 5'-triphosphate + 2,2-dichloroethanol
adenosine 5'-monophosphate-O-2,2-dichloroethyl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + 2-chloroethanol
adenosine 5'-monophosphate-O-2-chloroethyl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + ethylene glycol
adenosine 5'-monophosphate-O-ethylene glycyl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + glycerol
adenosine 5'-monophosphate-O-glyceryl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + glycerol-2-phosphate
adenosine 5'-monophosphate-O-glyceryl-2-phosphate ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + glycerol-3-phosphate
adenosine 5'-monophosphate-O-glyceryl-3-phosphate ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + methanol
adenosine 5'-monophosphate-O-methyl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
adenosine 5'-triphosphate + propanol
adenosine 5'-monophosphate-O-propyl ester + H2O + diphosphate
show the reaction diagram
-
-
-
ir
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
?
show the reaction diagram
bis(p-nitrophenyl)-phosphate + H2O
?
show the reaction diagram
-
-
-
?
bis(p-nitrophenyl)phosphate + H2O
?
show the reaction diagram
good substrate
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
cAMP + H2O
?
show the reaction diagram
-
very low activity
-
-
?
dinucleotide monophosphates + H2O
nucleoside + nucleoside 5'-monophosphate
show the reaction diagram
-
with 2'-5', 3'-5', or 5'-5' linkages
-
?
dinucleotides with 3'-phosphoryl terminus + H2O
nucleosides + 3',5'-diphosphonucleotides
show the reaction diagram
-
-
-
?
methyl esters of arabinose 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
nicotinamide adenine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
nicotinamide guanine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
oligonucleotides with 3'-phosphoryl terminus + H2O
nucleosides + 3',5'-diphosphonucleotides
show the reaction diagram
-
-
-
?
p-nitrophenyl thymidine 5'-phosphate + H2O
5'-TMP + p-nitrophenol
show the reaction diagram
-
-
-
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
show the reaction diagram
phenyl esters of arabinose 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
polynucleotide + H2O
5'-nucleotides
show the reaction diagram
thymidine-5'-phosphate 4-nitrophenyl ester + H2O
?
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activates
Ni2+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-([4-deoxy-4-(hydroxymethyl)-3-O-(phenylcarbonyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
-
IC50: 0.171 mM
2-([4-deoxy-4-(hydroxymethyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
-
IC50: 0.544 mM
2-mercaptoethanol
-
10 mM, 20% of inhibition
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)((E)-2-phenylethenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-indol-2-yl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-pyrol-2-yl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-bromophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-chlorophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-methoxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-pyridinyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-thienyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4-dimethoxyphenyl) methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-aminophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-chlorophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-ethoxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-hydroxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-nitrophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-pyridinyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-thienyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-hydroxy-3-ethoxyphenyl) methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-isopropylphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-methoxyphenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-N,N-dimethylaminophenyl) methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-nitrophenyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
-
-
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl]-2H-chromen-2-one
-
-
8-Hydroxy-5-quinoline sulfonic acid
-
-
ADP
-
competitive inhibition
benzoyl salireposide
-
shows strong inhibitory activity
Cu2+
-
required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity
CuSO4
-
10 mM, 90% of inhibition
cysteine
Dimerized thymine
dipicolinic acid
-
-
dithiothreitol
-
inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
glutathione
L-ascorbate
-
endogenous inhibitor, inhibits the phosphodiesterase activity of the enzyme through reduction of Cu2+
L-cysteine
-
-
MgSO4
-
100 mM, 40% of inhibition
MnCl2
-
10 mM, 50% of inhibition
o-phenanthroline
-
-
polyclonal antibodies
-
-
-
quinovic acid
snake
-
50% inhibition at 0.166 mM
quinovic acid 3-O-(beta-D-glucopyranoside)
snake
-
50% inhibition at 0.374 mM
quinovic acid-3-O-alpha-L-rhamnopyranoside
-
significant inhibitory activity against the enzyme
quinovic acid-3-O-beta-D-fucopyranoside
-
significant inhibitory activity against the enzyme
quinovic acid-3-O-beta-D-glucopyranosyl (1-> 4)-beta-D-fucopyranoside
-
significant inhibitory activity against the enzyme
salireposide
-
shows moderate inhibitory activity
symplomoside
-
shows weak inhibitory activity
symploracemoside
-
shows moderate inhibitory activity
thioglycolic acid
-
-
tris(2-carboxyethyl)phosphine
-
inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
additional information
-
calf intestine alkaline phosphatase-independent SVPD termini are piperidine resistant
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme reaction is induced by a ubiquitous pollutant acrolein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.091
ADP
-
pH 7.4, 37C
0.36
ATP
-
pH 7.4, 37C
2.69
bis(p-nitrophenyl)-phosphate
-
37C, pH 8.9
1.8
bis-p-nitrophenyl phosphate
-
-
0.23 - 1.82
dinucleotides
-
depending on nucleobase and presence of Mg2+
-
0.24
nicotinamide adenine dinucleotide
-
pH 7.4, 37C
0.29
nicotinamide guanine dinucleotide
-
pH 7.4, 37C
0.03
thymidine 5'-p-nitrophenyl phosphate
-
-
0.026 - 0.65
uridine oligonucleotides
-
with different degrees of polymerization
-
additional information
additional information
-
kinetics of purified native enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
ADP
Trimeresurus stejnegeri
-
pH 7.4, 37C
2.68
ATP
Trimeresurus stejnegeri
-
pH 7.4, 37C
0.82
nicotinamide adenine dinucleotide
Trimeresurus stejnegeri
-
pH 7.4, 37C
3.65
nicotinamide guanine dinucleotide
Trimeresurus stejnegeri
-
pH 7.4, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
ADP
Trimeresurus stejnegeri
-
pH 7.4, 37C
13
7.4
ATP
Trimeresurus stejnegeri
-
pH 7.4, 37C
4
3.5
nicotinamide adenine dinucleotide
Trimeresurus stejnegeri
-
pH 7.4, 37C
30278
12.6
nicotinamide guanine dinucleotide
Trimeresurus stejnegeri
-
pH 7.4, 37C
2662
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.525
2-([4-deoxy-4-(hydroxymethyl)-3-O-(phenylcarbonyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
-
-
1.1
2-([4-deoxy-4-(hydroxymethyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
-
-
0.525
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)((E)-2-phenylethenyl)methyl]-2H-chromen-2-one
-
-
1.05
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-indol-2-yl)methyl]-2H-chromen-2-one
-
-
0.0545
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-pyrol-2-yl)methyl]-2H-chromen-2-one
-
-
0.475
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-bromophenyl) methyl]-2H-chromen-2-one
-
-
0.45
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-chlorophenyl)methyl]-2H-chromen-2-one
-
-
0.35
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-thienyl)methyl]-2H-chromen-2-one
-
-
0.225
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-chromen-2-one
-
-
0.0545
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4-dimethoxyphenyl)methyl]-2H-chromen-2-one
-
-
0.5
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-aminophenyl)methyl]-2H-chromen-2-one
-
-
0.35
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-chlorophenyl)methyl]-2H-chromen-2-one
-
-
0.225
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-ethoxyphenyl)methyl]-2H-chromen-2-one
-
-
0.0125
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-hydroxyphenyl)methyl]-2H-chromen-2-one
-
-
0.9
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
-
-
0.35
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-nitrophenyl)methyl]-2H-chromen-2-one
-
-
0.15
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-pyridinyl)methyl]-2H-chromen-2-one
-
-
0.45
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-thienyl)methyl]-2H-chromen-2-one
-
-
0.125
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-hydroxy-3-ethoxyphenyl)methyl]-2H-chromen-2-one
-
-
1.1
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-methoxyphenyl)methyl]-2H-chromen-2-one
-
-
0.075
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-N,N-dimethylaminophenyl)methyl]-2H-chromen-2-one
-
-
1.115
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-nitrophenyl)methyl]-2H-chromen-2-one
-
-
0.15 - 0.9
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
0.375
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
-
-
0.008
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl]-2H-chromen-2-one
-
-
0.8
ADP
-
pH pH 9.0, 37C
6.2
cysteine
-
pH pH 9.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.171
2-([4-deoxy-4-(hydroxymethyl)-3-O-(phenylcarbonyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
Bothrops atrox
-
IC50: 0.171 mM
0.544
2-([4-deoxy-4-(hydroxymethyl)-beta-D-glucopyranosyl]oxy)-5-hydroxybenzyl benzoate
Bothrops atrox
-
IC50: 0.544 mM
0.2016
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)((E)-2-phenylethenyl) methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.4129
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-indol-2-yl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.0685
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(1H-pyrol-2-yl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.4166
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-bromophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.382
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-chlorophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
1
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-methoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
1
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-pyridinyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.654
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(2-thienyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.4131
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.0731
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3,4-dimethoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.4067
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-aminophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.3008
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-chlorophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.3048
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-ethoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.01334
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-hydroxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.4871
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-methoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.2579
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-nitrophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.0613
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-pyridinyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.753
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(3-thienyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.1752
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-hydroxy-3-ethoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
1
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-isopropylphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.6522
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-methoxyphenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.1095
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-N,N-dimethylaminophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.6
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-nitrophenyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.1474 - 0.678
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
0.301
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)ethyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.00944
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
8.3
ADP
Walterinnesia aegyptia
-
pH pH 9.0, 37C
0.171
benzoyl salireposide
Crotalus adamanteus
-
-
2.6
cysteine
Walterinnesia aegyptia
-
pH pH 9.0, 37C
6.9 - 8.62
dithiothreitol
2.56 - 3.45
glutathione
2.87
L-ascorbate
Trimeresurus stejnegeri
-
holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37C
0.544
salireposide
Crotalus adamanteus
-
-
0.998
symplomoside
Crotalus adamanteus
-
-
0.59
symploracemoside
Crotalus adamanteus
-
-
1.48 - 1.84
tris(2-carboxyethyl)phosphine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
per mg of venom
0.02
-
per mg of venom
0.024
-
per mg of venom
0.026
-
per mg of venom
0.027
-
per mg of venom
0.028
-
per mg of venom
0.037
-
per mg of venom
0.039
-
per mg of venom
0.042
-
per mg of venom
0.043
Bothrops pradoi
-
per mg of venom
0.044
-
per mg of venom
0.045
-
per mg of venom
0.048
-
per mg of venom
0.049
-
per mg of venom
0.051
-
per mg of venom
0.062
-
per mg of venom
0.067
-
per mg of venom
0.071
-
per mg of venom
0.075
-
per mg of venom
0.078
-
per mg of venom
0.079
-
per mg of venom
0.087
-
per mg of venom
0.093
-
per mg of venom
0.11
-
per mg of venom
1.3
-
purified native enzyme, substrate nicotinamide guanine dinucleotide, pH 7.4, 37C
3.4
-
purified native enzyme, pH 9.0, 37C
11.2
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
substrate oligonucleotides with 3'-monophosphoryl groups
7.5 - 9.5
-
-
7.5 - 9
-
assay at, dependent on the substrate
8.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 55
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 90
-
assay range, rapid loss of activity above 65C
65
-
up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.87
sequence calculation
7.48
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
reduced enzyme
93860
sequence calculation
105000
-
PAGE
112000
-
? * 112000, SDS-PAGE
115000
-
non-denaturing PAGE
120000
134000
-
? * 134000, SDS-PAGE
140000
-
? * 140000, SDS-PAGE
150000
158000
-
x * 158000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
the enzyme is synthesized as a 828-amino acid single-chain protein but subsequently cleaved to form a two-chain protein held together with disulfide bonds, nevertheless the enzyme behaves like a heterodimeric protein with 60000 kDa subunits, molecular modelling. The enzyme contains four domains including two somatomedin-B domains, a PDE/nucleotide pyrophosphatase domain, and a nonspecific endonuclease domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
lipoprotein
-
triacylglycerols 1.54%, cholesterol esters 1.13%
proteolytic modification
the enzyme is synthesized as a 828-amino acid single-chain protein but subsequently cleaved to form a two-chain protein held together with disulfide bonds
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.8
-
stable above
134117
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
denaturation above
70
-
1 min, complete loss of activity
75
-
denaturation above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
glycerol stabilizes
homologous antibody stabilizes
-
immobilization, on Concanavalinn-A-Sepharose, stabilization
-
instability of the enzyme in aqueous solution
-
repeated freeze-thaw cycles lead to loss of enzyme activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-17C, 0.2 M ammonium acetate buffer, pH 6.0, protein concentration less than 2 mg/ml
-
-20C, 0.1-0.5 mg/ml bovine serum albumin, more than 1 month
-20C, 30% glycerol
-
-7C, dilute solutions, 7 days, 3% activity
-
0C, diluted solutions, 2 months, 50% activity
-
25C, 0.1 M NaOH-glycine, pH 8.9, 72 h, stable
-
37C, 0.1 M NaOH-glycine, pH 8.9, 72 h, stable
-
4C, 0.1 M NaOH-glycine, pH 8.9, 72 h, stable
-
4C, 0.5-2 mg/ml, several weeks
-
4C, 10 mM Mg2+, serum albumin, more than 20 months
-
frozen, pH 6, or pH 9, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
50% pure
-
native enzyme 3fold from venom by preparative native polyacrylamide gel electrophoresis
-
native enzyme from venom by ion exchange chromatography and gel filtration to homogeneity
-
native extracellular enzyme from venom 3.2fold by gel filtration, and two different steps of anion exchange chromatography
removal of 5'-nucleotidase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
immobilization of the enzyme on the capillary monolith, method, overview. The immobilization of the enzyme facilitates the elimination or repression of the metal adducts of oligodeoxynucleotides during the enzyme reaction
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
some phenolic glycoside derivatives show inhibitory activity against snake venom phosphodiesterase I. Compounds are potential candidates for the therapy of snake bites
molecular biology
-
the enzyme is useful for production of the mass ladders of oligodeoxynucleotides with a single nucleotide difference, which can be produced, allowing for MS-based sequencing, construction of a capillary monolithic bioreactor constructed for the immobilized enzyme and handling (sub)microliter DNA samples