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Information on EC 3.1.15.1 - venom exonuclease
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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
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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
-
-
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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
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-82-5
-
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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
-
-
?
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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
-
-
?
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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
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme reaction is induced by a ubiquitous pollutant acrolein
-
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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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE