Any feedback?
Information on EC 3.1.15.1 - venom exonuclease
for references in articles please use BRENDA:EC3.1.15.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.15.1 venom exonucleaseSpecify your search results
Word Map
- 3.1.15.1
-
lysophosphatidic
- lysophospholipase
- lysophosphatidylcholine
- duplex
- endonuclease
- strand
- metastasis
- fibrosis
- rnase
-
single-stranded
- nucleases
- lysophospholipids
- polymerases
- polynucleotide
- phosphorothioate
- 5'-nucleotidase
- adp-ribose
-
adp-ribosylation
- oligodeoxynucleotides
- pruritus
- adp-ribosyltransferase
- oligodeoxyribonucleotides
-
itch
- phosphodiesterases
-
dinucleoside
-
exonucleolytic
-
ectonucleotide
-
internucleotide
-
phosphoramidite
-
proofreading
- deoxyribonuclease
-
nucleolytic
- 3'-terminus
- deoxynucleoside
- medicine
- oligoribonucleotides
-
micrococcal
-
abasic
- molecular biology
-
lpa-induced
-
32p-postlabeling
-
klenow
-
nuclease-resistant
- adamanteus
-
postlabeling
The enzyme appears in viruses and cellular organisms
Synonyms
autotaxin, snake venom phosphodiesterase, 3'-exonuclease, 5'-exonuclease, alkaline phosphodiesterase, 5'-nucleotide phosphodiesterase, venom phosphodiesterase, pde-i, snake venom phosphodiesterase i, venom exonuclease, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-exonuclease
-
-
-
-
5'-nucleotide phosphodiesterase
-
-
-
-
alkaline phosphodiesterase
-
-
-
-
autotaxin
-
-
-
-
Crotalus adamenteus venom exonuclease
-
-
-
-
posphodiesterase I
-
-
-
-
snake venom phosphodiesterase
snake venom phosphodiesterase I
venom phosphodiesterase
-
-
-
-
snake venom phosphodiesterase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates
preference for single-stranded substrate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9025-82-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-(dCTTCA-(2'-azetidine)T-TTTTTCTTC)-3' + H2O
?
-
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
?
-
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
?
-
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
?
-
for 2'-O-methyl-T modified antisense oligonucleotide 6 degradation goes faster with respect to the antisense oligonucleotides 2-5
-
-
?
5'-(dCTTCATT-(2'-azetidine)T-TTTCTTC)-3' + H2O
?
-
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
?
-
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
?
-
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
?
-
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
?
-
azetidine-T modified antisense oligonucleotide 8 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTTTTC-(2'-N-4'-C-ethylene-bridged)T-TC)-3' + H2O
?
-
2'-N,4'-C-ethylene-bridged nucleic acid thymidine modified antisense oligonucleotide 2 still remains undegraded to certain extent
-
-
?
5'-(dCTTCATTTTTTCTTC)-3' + H2O
?
-
unmodified antisense oligonucleotide 1 is completely degraded after 30 min
-
-
?
adenosine 5'-monophosphate-O-ethyl ester + H2O
adenosine 5'-monophosphate + ethanol
-
-
-
ir
adenosine 5'-O-phosphorothioate-O-p-nitrophenyl ester + H2O
adenosine-5'-O-phosphorothioate + p-nitrophenol
adenosine 5'-triphosphate + 2,2-dichloroethanol
adenosine 5'-monophosphate-O-2,2-dichloroethyl ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + 2-chloroethanol
adenosine 5'-monophosphate-O-2-chloroethyl ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + ethylene glycol
adenosine 5'-monophosphate-O-ethylene glycolyl ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + glycerol
adenosine 5'-monophosphate-O-glyceryl ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + glycerol-2-phosphate
adenosine 5'-monophosphate-O-glyceryl-2-phosphate ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + glycerol-3-phosphate
adenosine 5'-monophosphate-O-glyceryl-3-phosphate ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + methanol
adenosine 5'-monophosphate-O-methyl ester + H2O + diphosphate
-
-
-
ir
adenosine 5'-triphosphate + propanol
adenosine 5'-monophosphate-O-propyl ester + H2O + diphosphate
-
-
-
ir
dinucleotide monophosphates + H2O
nucleoside + nucleoside 5'-monophosphate
-
with 2'-5', 3'-5', or 5'-5' linkages
-
?
dinucleotides with 3'-phosphoryl terminus + H2O
nucleosides + 3',5'-diphosphonucleotides
-
-
-
?
oligonucleotides with 3'-phosphoryl terminus + H2O
nucleosides + 3',5'-diphosphonucleotides
-
-
-
?
p-nitrophenyl thymidine 5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
-
-
-
?
4-nitrophenyl thymidine-5'-phosphate + H2O
4-nitrophenol + thymidine-5'-phosphate
-
-
-
-
?
4-nitrophenyl thymidine-5'-phosphate + H2O
4-nitrophenol + thymidine-5'-phosphate
best substrate
-
-
?
adenosine 5'-O-phosphorothioate-O-p-nitrophenyl ester + H2O
adenosine-5'-O-phosphorothioate + p-nitrophenol
-
-
-
?
adenosine 5'-O-phosphorothioate-O-p-nitrophenyl ester + H2O
adenosine-5'-O-phosphorothioate + p-nitrophenol
Crotalus terrificus terrificus
-
-
-
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
-
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
p-nitrophenylthymidine-5'-phosphate + H2O
5'-TMP + p-nitrophenol
-
requirement of 3'-hydroxyl group
-
?
polynucleotide + H2O
5'-nucleotides
-
no hydrolysis of nuceotides in syn configuration
-
?
additional information
?
-
-
3' strand-break termini can be digested by SVPD. Strand-break termini can be recognized directly and digested by SVPD without calf intestine alkaline phosphatase pretreatment, whereas other termini cannot be digested by SVPD without calf intestine alkaline phosphatase pretreatment
-
-
?
additional information
?
-
-
digests 70-kDa protein of the clinical Helicobacter pylori isolate OMH4 and 55-kDa and 45-kDa proteins of human gastric carcinoma, releases only AMP
-
-
?
additional information
?
-
-
oligodeoxynucleotides containing 1,8-naphthyridine C-nucleoside and imidazo[5',4':4,5]pyrido[2,3-d]pyrimidine nucleoside at the terminal positions are 6-40times more resistant than natural DNA to SVPD digestion despite possessing a natural phosphodiester linkage
-
-
?
additional information
?
-
-
the enzyme has the unique ability as an exonuclease to sequentially cleave one nucleotide from single-stranded DNA, MALDI-TOF mass spectrometric analysis of reaction products
-
-
?
additional information
?
-
-
alcohol competes with water in esterification, so that adenosine 5'monophosphate can also be a product
-
-
?
additional information
?
-
-
alcohol competes with water in esterification, so that adenosine 5'monophosphate can also be a product
-
-
?
additional information
?
-
the enzyme hydrolyses ADP but not ATP and 5'-AMP, the enzyme inhibits aggregation of platelets induced by ADP or collagen
-
-
?
additional information
?
-
-
the enzyme hydrolyses ADP but not ATP and 5'-AMP, the enzyme inhibits aggregation of platelets induced by ADP or collagen
-
-
?
additional information
?
-
-
the enzyme also exhibits DNase activity
-
-
?
additional information
?
-
-
the purified enzyme TS-PDE exhibits exonuclease activity with a broad phosphodiesterase substrate range with the descending order of specificity: nicotinamide guanine dinucleotide, ATP, nicotinamide adenine dinucleotide, ADP
-
-
?
additional information
?
-
-
the enzyme sequentially removes mononucleotide units from the polynucleotide chain starting from the free 3' hydroxyl end, and can attack DNA, RNA, or any nucleotide chain
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme has the unique ability as an exonuclease to sequentially cleave one nucleotide from single-stranded DNA, MALDI-TOF mass spectrometric analysis of reaction products
-
-
?
additional information
?
-
-
the enzyme also exhibits DNase activity
-
-
?
additional information
?
-
-
the enzyme sequentially removes mononucleotide units from the polynucleotide chain starting from the free 3' hydroxyl end, and can attack DNA, RNA, or any nucleotide chain
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Mg2+
Zn2+
additional information
Cu2+
-
required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity
additional information
-
analysis of the effects of metal ions and small-molecule reductants on the enzyme's structure and activity, overview. Mg2+, Mn2+, Ni2+, Co2+ and Ca2+ can partiallyy substitute for Cu2+ and Zn2+
additional information
-
the enzyme is active in the absence of any divalent ions and the addition of Ca2+ or Mg2+ has no significant effect on the activity of Walterinnesia aegyptia PDE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
-
Cu2+
-
required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity
dithiothreitol
-
inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
L-ascorbate
-
endogenous inhibitor, inhibits the phosphodiesterase activity of the enzyme through reduction of Cu2+
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
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
-
EDTA
-
strong inhibition, addition of 10 mM Ca2+ restored only 8% of the enzyme activity
glutathione
-
endogenous inhibitor, inhibits the phosphodiesterase activity of the enzyme by reducing both the Cu2+ and disulfide bonds
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme reaction is induced by a ubiquitous pollutant acrolein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23 - 1.82
dinucleotides
-
depending on nucleobase and presence of Mg2+
-
0.026 - 0.65
uridine oligonucleotides
-
with different degrees of polymerization
-
additional information
additional information
-
kinetics of purified native enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
-
0.15
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
-
-
0.9
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
-
2.87
L-ascorbate
Trimeresurus stejnegeri
-
holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C
0.1474
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
0.678
4-hydroxy-3-[(4-hydroxy-2-oxo-2H-chromen-3-yl)(4-pyridinyl)methyl]-2H-chromen-2-one
Crotalus adamanteus
-
-
6.9
dithiothreitol
Trimeresurus stejnegeri
-
holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C
2.56
glutathione
Trimeresurus stejnegeri
-
holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C
1.48
tris(2-carboxyethyl)phosphine
Trimeresurus stejnegeri
-
holo-enzyme containing Cu2+ and Zn2+, pH 7.4, 37°C
1.84
tris(2-carboxyethyl)phosphine
Trimeresurus stejnegeri
-
enzyme containing only Zn2+, pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
0.006
0.007
0.008
0.009
0.01
0.012
0.013
0.014
0.015
0.016
0.017
0.018
0.019
0.031
0.033
0.05
0.052
1.3
-
purified native enzyme, substrate nicotinamide guanine dinucleotide, pH 7.4, 37°C
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the phosphodiesterase TS-PDE strongly inhibits ADP-induced platelet aggregation in human plateletrich plasma by hydrolyzing ADP
additional information
additional information
enzyme secondary structure molecular modelling
additional information
-
the catalytic activity of the enzyme relies on its disulfide bonds and bimetallic cluster
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDE_MACLB
851
0
96181
Swiss-Prot
other Location (Reliability: 3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
150000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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
glycoprotein
-
neutral sugars 9.2%, amino sugars 1.9%, 10 sialic acid residues per molecule
glycoprotein
-
the venom phosphodiesterase TS-PDE is a glycoprotein which contains 2.48% carbohydrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
glycerol stabilizes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-17°C, 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kini, R.M.; Gowda, T.V.
Rapid method for separation and purification of four isoenzymes of phosphodiesterase from Trimeresurus flavoviridis (Habu snake) venom
J. Chromatogr.
291
299-305
1984
Protobothrops flavoviridis, Protobothrops flavoviridis Habu
brenda
Pollack, S.E.; Uchida, T.; Auld, D.S.
Snake venom phosphodiesterase: A zinc metalloenzyme
J. Protein Chem.
2
1-12
1983
Crotalus adamanteus
-
brenda
Dolapchiev, L.B.; Vassileva, R.A.; Koumanov, K.S.
Venom exonuclease. II. Amino acid composition and carbohydrate, metal ion and lipid content in the Crotalus adamanteus venom exonuclease
Biochim. Biophys. Acta
622
331-336
1980
Crotalus adamanteus
brenda
Dolapchiev, L.B.; Vassiliev, L.T.
Venom exonuclease. III. Immunochemical characterization and modification by specific antibody
Biochim. Biophys. Acta
667
355-360
1981
Crotalus adamanteus
brenda
Tin-Win; Aye-Kyaw; Sanda; San-Aye; Win-Aung; Khin-Pa-Pa-Kyaw; Aung-Myat-Kyaw
Purification, characterization and biological properties of phosphodiesterase from Russel's viper (Vipera russelli) venom
The Snake
28
83-89
1998
Daboia siamensis
-
brenda
Dolapchiev, L.B.
Venom exonuclease-kinetics and specificity towards different nucleotide substrates
Int. J. Biol. Macromol.
2
7-12
1980
Crotalus adamanteus
-
brenda
Oka, J.; Ueda, K.; Hayaishi, O.
Snake venom phosphodiesterase: simple purification with Blue Sepharose and its application to poly(ADP-ribose) study
Biochem. Biophys. Res. Commun.
80
841-848
1978
Crotalus adamanteus, Crotalus atrox
brenda
Ballario, P.; Bergami, M.; Pedone, F.
A simple method for the purification of phosphodiesterase from Vipera aspis venom
Anal. Biochem.
80
646-651
1977
Vipera aspis
brenda
Philipps, G.R.
Purification and characterization of phosphodiesterase I from Bothrops atrox
Biochim. Biophys. Acta
432
237-244
1976
Bothrops atrox
brenda
Ogilvie, K.K.; Hruska, F.H.
Affect of spleen and snake venom phosphodiesterases on nucleotides containing nucleosides in the syn conformation
Biochem. Biophys. Res. Commun.
68
375-378
1976
Crotalus adamanteus
brenda
Philipps, G.R.
Purification and characterization of phosphodiesterase from Crotalus venom
Hoppe-Seyler's Z. Physiol. Chem.
356
1085-1096
1975
Crotalus adamanteus, Crotalus terrificus terrificus
brenda
Eckstein, F.; Frischauf, A.M.
Affinity chromatography of phosphodiesterase from snake venom
Methods Enzymol.
34
605-610
1974
Bothrops atrox, Crotalus adamanteus
brenda
Petrovaa, M.; Philippsen, P.; Zachau, H.G.
Partial degradation of transfer RNAs by different preparations of snake venom exonuclease
Biochim. Biophys. Acta
395
455-467
1975
Bothrops atrox, Crotalus adamanteus, Macrovipera lebetina, Daboia siamensis
brenda
Stulberg, M.P.; Isham, K.R.
The production of limit-oligonucleotide digests from phenylalanine tRNA (Escherichia coli) with snake venom phosphodiesterase
Methods Enzymol.
29E
477-482
1974
Crotalus adamanteus
brenda
Sulkowski, E.; Laskowski, M.Sr.
Venom exonuclease (phosphodiesterase) immobilized on concanavalin-A-sepharose
Biochem. Biophys. Res. Commun.
57
463-468
1974
Crotalus adamanteus
brenda
Frischauf, A.M.; Eckstein, F.
Purification of a phosphodiesterase from Bothrops atrox venom by affinity chromatography
Eur. J. Biochem.
32
479-485
1973
Bothrops atrox
brenda
Sulkowski, E.; Laskowski, M.Sr.
Inactivation of 5'-nucleotidase in commercial preparations of venom exonuclease (phosphodiesterase)
Biochim. Biophys. Acta
240
443-447
1971
Crotalus adamanteus
-
brenda
Richards, G.M.; Laskowski, M.Sr.
Negative charge at the 3 terminus of oligonucleotides and resistance to venom exonuclease
Biochemistry
8
1786-1795
1969
Crotalus adamanteus
brenda
Hadjiolov, A.A.; Venkov, P.V.; Dolapchiev, L.B.; Genchiev, D.D.
The action of snake venom phosphodiesterase on liver ribosomal ribonucleic acids
Biochim. Biophys. Acta
142
111-127
1967
Crotalus adamanteus
brenda
Dolapchiev, L.B.; Sulkowski, E.; Laskowski, M.Sr.
Purification of exonuclease (phosphodiesterase) from the venom of Crotalus adamanteus
Biochem. Biophys. Res. Commun.
61
273-281
1974
Crotalus adamanteus
brenda
Richards, G.M.; Tutas, D.J.; Wechter, W.J.; Laskowski, M.Sr.
Hydrolysis of dinucleoside monophosphates containing arabinose in various internucleotide linkages by exonuclease from the venom of Crotalus adamanteus
Biochemistry
6
2908-2914
1967
Crotalus adamanteus
brenda
Stoynov, S.S.; Bakalova, A.T.; Dimov, S.I.; Mitkova, A.V.; Dolapchiev, L.B.
Single-strand-specific DNase activity is an inherent property of the 140-kDa protein of the snake venom exonuclease
FEBS Lett.
409
151-154
1997
Crotalus adamanteus
brenda
Garcia-Diaz, M.; Avalos, M.; Cameselle, J.C.
Alcohol esterification reactions and mechanisms of snake venom 5'-nucleotide phosphdiesterase
Eur. J. Biochem.
213
1139-1148
1993
Crotalus durissus terrificus
brenda
Laskowski, M.Sr.in
Exonuclease (phosphodiesterase) and other nucleolytic enzymes from venom
Procedures in Nucleic Acid Research (Cantoni, G. L. ; Davies, D. R. , eds. )
154-184
1966
Bothrops atrox, Bungarus multicinctus, Crotalus adamanteus, Daboia siamensis, Deinagkistrodon acutus, Hemachatus haemachatus, Naja atra, Protobothrops mucrosquamatus, Trimeresurus gramineus
-
brenda
Vergeles, J.M.; Garcia-Diaz, M.; Cemeselle, J.C.
High efficiency of glycerol 2-phosphate and sn-glycerol 3-phosphate as nucleotidyl acceptors in snake venom phophodiesterase esterifications. Formation of primary and secondary AMP-O-glyceryl and AMP-O-glycerophosphoryl esters and evidence for an acceptor-binding enzyme site
Eur. J. Biochem.
223
442-447
1995
Crotalus durissus terrificus
-
brenda
Bugers, P.M.; Eckstein, F.
Hunneman, D.H.: Stereochemistry of hydrolysis by snake venom phosphodiesterase
J. Biol. Chem.
254
7476-7478
1979
Crotalus terrificus terrificus
brenda
Valerio, A.A.; Corradini, A.C.; Panunto, P.C.; Mello, S.M.; Hyslop, S.
Purification and characterization of a phosphodiesterase from Bothrops alternatus snake venom
J. Protein Chem.
21
495-503
2002
Bothrops alternatus
brenda
Fatima, N.; Tapondjou, L.A.; Lontsi, D.; Sondengam, B.L.; Atta Ur, R.; Choudhary, M.I.
Quinovic acid glycosides from Mitragyna stipulosa--first examples of natural inhibitors of snake venom phosphodiesterase I
Nat. Prod. Lett.
16
389-393
2002
snake
brenda
Choudhary, M.I.; Fatima, N.; Abbasi, M.A.; Jalil, S.; Ahmad, V.U.; Atta ur, R.
Phenolic glyscosides, a new class of human recombinant nucleotide pyrophosphatase phosphodiesterase-1 inhibitors
Bioorg. Med. Chem.
12
5793-5798
2004
Bothrops atrox
brenda
Aird, S.D.
Taxonomic distribution and quantitative analysis of free purine and pyrimidine nucleosides in snake venoms
Comp. Biochem. Physiol. B
140
109-126
2005
Deinagkistrodon acutus, Gloydius blomhoffii, Calloselasma rhodostoma, Bitis gabonica, Bothrops asper, Bothrops atrox, Bothrops jararaca, Bothrops moojeni, Bungarus fasciatus, Crotalus adamanteus, Crotalus atrox, Echis carinatus, Eristicophis macmahoni, Naja melanoleuca, Naja naja, Naja atra, Naja oxiana, Ophiophagus hannah, Daboia russelii, Vipera aspis, Macrovipera lebetina, Bothrops jararacussu, Naja mossambica, Bothrops alternatus, Naja kaouthia, Naja sputatrix, Bitis arietans, Crotalus durissus, Naja nivea, Agkistrodon bilineatus, Agkistrodon piscivorus, Bothrops bilineatus, Bothriechis schlegelii, Bothrops cotiara, Bothrops neuwiedi, Bothrops pradoi, Crotalus horridus, Crotalus basiliscus, Crotalus cerastes, Crotalus molossus, Crotalus ruber, Crotalus scutulatus, Crotalus cerberus, Crotalus oreganus concolor, Naja haje, Crotalus oreganus helleri, Crotalus oreganus lutosus, Crotalus oreganus oreganus, Crotalus viridis viridis, Gloydius halys ussuriensis, Hypnale hypnale, Porthidium lansbergii, Porthidium nasutum, Atropoides nummifer, Sistrurus tergeminus, Sistrurus miliarius barbouri, Bitis nasicornis, Causus rhombeatus, Cerastes vipera, Pseudocerastes persicus, Vipera ammodytes, Vipera berus, Vipera latastei, Daboia palaestinae, Montivipera xanthina, Naja pallida, Naja nigricollis
brenda
Akamatsu, K.
A novel methodology for characterizing strand-break termini and damaged bases in plasmid DNA exposed to ionizing radiation
Anal. Biochem.
362
229-235
2007
Crotalus adamanteus
brenda
Honcharenko, D.; Barman, J.; Varghese, O.P.; Chattopadhyaya, J.
Comparison of the RNase H cleavage kinetics and blood serum stability of the north-conformationally constrained and 2-alkoxy modified oligonucleotides
Biochemistry
46
5635-5646
2007
Crotalus adamanteus
brenda
Choudhary, M.I.; Fatima, N.; Khan, K.M.; Jalil, S.; Iqbal, S.; Atta-Ur-Rahman, S.
New biscoumarin derivatives-cytotoxicity and enzyme inhibitory activities
Bioorg. Med. Chem.
14
8066-8072
2006
Crotalus adamanteus
brenda
Huo, C.H.; Shen, L.R.; Zhao, Y.Y.; Liang, H.
Chemical constituents of plants from the genus Symplocos
Chem. Biodivers.
4
1-11
2007
Crotalus adamanteus
brenda
Hikishima, S.; Minakawa, N.; Kuramoto, K.; Ogata, S.; Matsuda, A.
Synthesis and characterization of oligodeoxynucleotides containing naphthyridine:imidazopyridopyrimidine base pairs at their sticky ends. Application as thermally stabilized decoy molecules
Chembiochem
7
1970-1975
2006
Crotalus adamanteus
brenda
Akai, T.; Nabeya, Y.; Yahiro, K.; Morinaga, N.; Mitsuhashi, K.; Inoue, M.; Sakamoto, A.; Ochiai, T.; Noda, M.
Helicobacter pylori induces mono-(adenosine 5-diphosphate)-ribosylation in human gastric adenocarcinoma
Int. J. Oncol.
29
965-972
2006
Crotalus adamanteus
brenda
Mostafa, M.; Nahar, N.; Mosihuzzaman, M.; Sokeng, S.D.; Fatima, N.; Atta-Ur-Rahman, N.; Choudhary, M.I.
Phosphodiesterase-I inhibitor quinovic acid glycosides from Bridelia ndellensis
Nat. Prod. Res.
20
686-692
2006
Crotalus adamanteus
brenda
Watts, J.K.; Katolik, A.; Viladoms, J.; Damha, M.J.
Studies on the hydrolytic stability of 2-fluoroarabinonucleic acid (2F-ANA)
Org. Biomol. Chem.
7
1904-1910
2009
Crotalus adamanteus
brenda
Dhananjaya, B.L.; D Souza, C.J.
An overview on nucleases (DNase, RNase, and phosphodiesterase) in snake venoms
Biochemistry (Moscow)
75
1-6
2010
Trimeresurus stejnegeri
brenda
Al-Saleh, S.S.; Khan, S.
Purification and characterization of phosphodiesterase I from Walterinnesia aegyptia venom
Prep. Biochem. Biotechnol.
41
262-277
2011
Walterinnesia aegyptia
brenda
Zhao, C.; Yin, R.; Yin, J.; Zhang, D.; Wang, H.
Capillary monolithic bioreactor of immobilized snake venom phosphodiesterase for mass spectrometry based oligodeoxynucleotide sequencing
Anal. Chem.
84
1157-1164
2012
Crotalus atrox
brenda
Trummal, K.; Aaspollu, A.; Tonismaegi, K.; Samel, M.; Subbi, J.; Siigur, J.; Siigur, E.
Phosphodiesterase from Vipera lebetina venom - structure and characterization
Biochimie
106
48-55
2014
Macrovipera lebetina (W8E7D1), Macrovipera lebetina
brenda
Peng, L.; Xu, X.; Guo, M.; Yan, X.; Wang, S.; Gao, S.; Zhu, S.
Effects of metal ions and disulfide bonds on the activity of phosphodiesterase from Trimeresurus stejnegeri venom
Metallomics
5
920-927
2013
Trimeresurus stejnegeri
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.1.15.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
