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Information on EC 3.1.21.7 - deoxyribonuclease V
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EC Tree
3.1.21.7 deoxyribonuclease VSpecify your search results
Word Map
- 3.1.21.7
- nick
-
deaminate
-
phosphodiester
-
beta-polymerase
-
deoxyinosine-containing
-
3\'-hydroxyl
-
proofreading
- biotechnology
- analysis
- molecular biology
- drug development
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
endo v, dnase v, deoxyinosine 3' endonuclease, agtendov, pfuendov, deoxyinosine 3'endonuclease, escherichia coli endodeoxyribonuclease v, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGTendoV
-
bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities
deoxyinosine 3' endonuclease
-
preferentially cleaves DNA containing deoxyinosine
Deoxyinosine 3'endonuclease
-
-
-
-
DNase V
-
-
-
-
EC 3.1.22.3
-
-
formerly
-
endo V
endodeoxyribonuclease V
-
-
-
-
endonuclease V
EndoV
Escherichia coli endodeoxyribonuclease V
-
-
-
-
nfi
Tb10.6k15.3890
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate
Previously classified erroneously as EC 3.1.22.3
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
61970-03-4
Previously classified erroneously as EC 3.1.22.3
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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
12-mer oligonucleotide + H2O
hydrolyzed DNA
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
?
34-mer oligonucleotide + H2O
fragments of 34mer-oligonucleotide
Tequatrovirus T4
-
oligonucleotide duplex containing a fluorine atom at the 2' position of the 5' component of the cyclobutane pyrimidine dimer
-
-
?
48-mer oligonucleotide + H2O
24-mer oligonucleotide
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
2,3-didehydro-2,3-dideoxyribose 5'-phosphate at the 3'-terminus of the products, initiation of repair synthesis by E. coli DNA-polymerase I
?
49-mer oligonucleotide + H2O
3-alpha,beta-unsaturated aldehyde + 3'-phosphate DNA-termini
Tequatrovirus T4
-
double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer, enzyme requires a secondary binding event after beta-elimination at a pyrimidine dimer or abasic site
delta-elimination reaction
?
deoxyinosine-containing RNA + H2O
?
(32)P-labeled 21-mer RNA substrate with inosine (5'-CUGUAUGAUGIAGAUGCUGAC-3'). EndoV is a deoxyinosine 3'-endonuclease that recognizes DNA containing deoxyinosine, and cleaves the second and third phosphodiester bonds 3' to the damaged base, leaving a nick with 3' hydroxyl and 5' phosphate groups. Human endonuclease V prefers RNA substrates with inosine over DNA substrates with deoxyinosine
-
-
?
deoxyinosine-containing single-stranded DNA + H2O
?
precursor activity of DNA repair
-
-
?
DNA + H2O
3-alpha,beta-unsaturated aldehyde + 5'-phosphate DNA-termini
Tequatrovirus T4
-
abasic lyase activity
-
?
dsDNA containing deoxyinosine + H2O
?
no cleavage activity is detected with the dsDNA containing a T/G mismatch base pair and a dsDNA containing an apurinic site. The enzyme possesses strict substrate specificity to deoxyinosine-containing DNA. The enzyme cleaves inosine-containing RNA strands as well as DNA substrates
-
-
?
single-stranded circular DNA + H2O
linearized single-stranded DNA
-
10fold more activity than for duplex DNA
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
also possesses abasic lyase activity
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
also possesses abasic lyase activity
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
also possesses abasic lyase activity
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
also possesses abasic lyase activity
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
?
49-mer oligonucleotide + H2O
hydrolysed DNA
Tequatrovirus T4
-
double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
?
deoxyinosine-containing deoxyoligonucleotide + H2O
?
the enzyme is involved in damaged DNA repair
-
-
?
deoxyinosine-containing deoxyoligonucleotide + H2O
?
the enzyme hydrolyzes the second phosphodiester bond 3' from deoxyinosine
-
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
cleavage of both denatured and native eukaryotic DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
also nicks duplex DNA exposed to OsO4, x-rays or acid, does not act upon undamaged DNA or irradiated single-stranded DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
cleaves deoxyinosine-containing DNA, urea residues-containing DNA, apurinic sites, base mismatches, insertion/deletion mismatches, flaps and pseudo-Y structures
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
active at apurinic/apyrimidinic sites, UV light induced damages, adducts of 7-bromomethylbenz(a)anthracene, uracil-containing duplex DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
-
-
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
two distinct activities: pyrimidine dimer glycosylase and apurinic-apyrimidinic endonuclease, beta-elimination of the 3'-phosphate of an abasic site
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific base excision repair pathway
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
moving a DNA base extrahelical opposite the target site that induces a conformational change to facilitate catalysis
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
endonuclease V repairs UV-induced cyclobutane pyrimidine dimers in DNA
-
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
EndoV hydrolyzes the second phosphodiester bond 3' of a deaminated base using Mg2+ as a cofactor
-
-
?
DNA + H2O
?
-
the enzyme nicks uracil-containing DNA at the seond or third phosphodiester bond 3' to uracil sites
-
-
?
DNA + H2O
?
-
the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
-
-
?
DNA + H2O
?
dI-containing heteroduplex DNAs are constructed, in which the dI resided in a disrupted restriction endonuclease recognition sites of bacteriophage M13mp18 DNA
-
-
?
DNA + H2O
?
the enzyme is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV
-
-
?
DNA + H2O
?
dI-containing heteroduplex DNAs are constructed, in which the dI resided in a disrupted restriction endonuclease recognition sites of bacteriophage M13mp18 DNA
-
-
?
DNA + H2O
?
Escherichia coli O45:K1/S88
the enzyme is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV
-
-
?
DNA + H2O
?
Escherichia coli O45:K1/S88/ExPEC
the enzyme is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV
-
-
?
DNA + H2O
?
-
the recombinant protein repais O6-methylguanine lesions in DNA via alkyl transfer action. The AGTendoV recombinant protein also cleaves DNA substrates that contain the deaminated bases uracil, hypoxanthine, or xanthine in a similar manner to Escherichia coli endonuclease V
-
-
?
DNA + H2O
?
5'-GCTCGGCTICGGACCGAG-3'. Endonuclease V is an inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine
-
-
?
DNA + H2O
?
endonuclease V recognizes deoxyinosine and cleaves the second phosphodiester bond on the 3' side of the deaminated base lesion in damaged DNA. The enzyme possesses specific endonuclease activity for the deoxyinosine-containing DNA strand
-
-
?
DNA + H2O
?
-
limited turnover on cleavage of deoxyinosine- and xanthosine-containing DNA. Nicking activity is similar between the double-stranded deoxyinosine- and deoxyxanthosine-containing DNA. Endonuclease V can only turnover deoxyuridine-containing DNA to a limited extent when substrate is in excess. Endonuclease V achieves tight binding to deoxyuridine-containing DNA. The active site of salmonella endonuclease V can accomodate pyrimidine-containing mismatches, resulting in more comparable cleavage of pyrimidine- and purine-containing mismatches. The plastic nature of the active site allows the enzyme to enfold both purine and pyrimidine deaminated lesions or base pair mismatches
-
-
?
DNA + H2O
?
-
limited turnover on cleavage of deoxyinosine- and xanthosine-containing DNA. Nicking activity is similar between the double-stranded deoxyinosine- and deoxyxanthosine-containing DNA. Endonuclease V can only turnover deoxyuridine-containing DNA to a limited extent when substrate is in excess. Endonuclease V achieves tight binding to deoxyuridine-containing DNA. The active site of salmonella endonuclease V can accomodate pyrimidine-containing mismatches, resulting in more comparable cleavage of pyrimidine- and purine-containing mismatches. The plastic nature of the active site allows the enzyme to enfold both purine and pyrimidine deaminated lesions or base pair mismatches
-
-
?
DNA + H2O
?
-
the enzyme can cleave oxanosine-containing DNA at the second phosphodiester bond 3' to the lesion. All four oxanosine-containing base pairs (A/O), T/O, C/O and G/O are cleaved with similar efficiency. The cleavage of double-stranded oxanosine-containing DNA is about 6fold less efficient than that of double-stranded inosine-containing DNA. Single-stranded oxanosine-containing DNA is cleaved with a lower efficiency as compared with double-stranded oxanosine-containing DNA
-
-
?
DNA + H2O
?
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
-
?
DNA + H2O
?
the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA
-
-
?
DNA + H2O
?
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
-
?
DNA + H2O
?
the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA
-
-
?
DNA + H2O
?
the enzyme binds A:TT loops with higher affinity than undamaged DNA
-
-
?
DNA + H2O
?
-
the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
-
-
?
DNA + H2O
?
the enzyme efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA-like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
DNA + H2O
?
the enzyme efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA-like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
DNA + H2O
hydrolysed DNA
cleavage of deaminated bases at the second phosphodiester bond 3' downstream to a lesion
-
-
?
DNA + H2O
hydrolysed DNA
hydrolysis of the second phosphodiester bond 3' from a deaminated base lesion including inosine, xanthosine, oxanosine and uridine
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
10fold lower activity than for single-stranded circular DNA, relaxed plasmid DNA, exposure to UV light or sodium bisulfite, to pH 5.2 or osmium tetroxide renders duplex DNA 7fold more active, best substrate is uracil containing DNA from Bacillus subtilis
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
removal of 3'deoxytermini
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
-
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
predominant release of a beta-elimination product rather than a hydrolytic product
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
RNA + H2O
?
the enzyme is active on RNA substrates containing one or several inosines. It does not cleave at inosines in DNA
-
-
?
RNA + H2O
?
the enzyme also cleaves inosine-containing RNA strands
-
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA
-
-
?
RNA-DNA hybrid + H2O
?
the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA. The enzyme cleaves an RNA substrate containing inosine in a position corresponding to a biologically important site for deamination in the Gabra-3 transcript of the GABAA neurotransmitter. Further, the enzyme specifically incises transfer RNAs with inosine in the wobble position
-
-
?
single-stranded RNA + H2O
?
5'-CUGACUICGGAUCAGGGCC-3'. The enzyme is most active towards single-stranded RNA but is much less active towards other substrates
-
-
?
single-stranded RNA + H2O
?
in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
-
-
?
single-stranded RNA + H2O
?
the enzyme efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA-like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
single-stranded RNA + H2O
?
in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
-
-
?
single-stranded RNA + H2O
?
the enzyme efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA-like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
ssRNA rI + H2O
?
efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
ssRNA rI + H2O
?
efficiently processes single-stranded RNA oligonucleotides with inosine, including A to I-edited tRNA like substrates but exhibits weak activity over DNA, except when a ribonucleotide is placed 3' to the inosine
-
-
?
additional information
?
-
-
the enzyme shows the repair reaction in vitro on M13mp18 derived heteroduplexes containing a site-specific deoxyinosine. Unpaired dI/G mismatch resides within the recognition site for XhoI restriction endonucleases, permitting evaluation of repair occurring on deoxyinosine-containing DNA strand
-
-
?
additional information
?
-
-
a dual enzymatic amplified strategy for the detection of EndoV activity based on a nicking enzyme and a template independent polymerase is developed
-
-
?
additional information
?
-
the enzyme shows affinity for but does not cleave branched DNA substrates like 5'-flap, 3'-flap, pseudo-Y, fork, 3-way junction, and Holliday junction
-
-
?
additional information
?
-
Tequatrovirus T4
-
endonuclease V detects apurinic/apyrimidinic site base paired with adenine and cyclobutane pyrimidine dimers in UV-damaged DNA
-
-
?
additional information
?
-
Tequatrovirus T4
-
enhanced cyclobutane pyrimidine dimer repair in UV-irradiated keratinocytes by T4 endonuclease V reduces the induction of matrix metalloproteinase-1 mRNA
-
-
?
additional information
?
-
-
3'-exonuclease activity in endonuclease V might be preferentially triggered by the specific cleavage event at the inosine site
-
-
?
additional information
?
-
EndoV cleaves substrates with base mismatches and helical distortions, such as mismatch loops, hairpins and flap structures, EndoV cleaves mismatched base pairs preferentially at adenine and guanine purines, EndoV binds to cleaved mismatch base pair products with much lower affinity as compared to cleaved deaminated bases
-
-
?
additional information
?
-
-
endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. But Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity and non-specific 5'-exonuclease activity
-
-
?
additional information
?
-
-
cleavage of 50-labeled inosine- and non-inosine-containing substrates
-
-
?
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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
deoxyinosine-containing deoxyoligonucleotide + H2O
?
the enzyme is involved in damaged DNA repair
-
-
?
RNA + H2O
?
the enzyme also cleaves inosine-containing RNA strands
-
-
?
single-stranded circular DNA + H2O
linearized single-stranded DNA
-
10fold more activity than for duplex DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
cleavage of both denatured and native eukaryotic DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
also nicks duplex DNA exposed to OsO4, x-rays or acid, does not act upon undamaged DNA or irradiated single-stranded DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
cleaves deoxyinosine-containing DNA, urea residues-containing DNA, apurinic sites, base mismatches, insertion/deletion mismatches, flaps and pseudo-Y structures
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
active at apurinic/apyrimidinic sites, UV light induced damages, adducts of 7-bromomethylbenz(a)anthracene, uracil-containing duplex DNA
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
two distinct activities: pyrimidine dimer glycosylase and apurinic-apyrimidinic endonuclease, beta-elimination of the 3'-phosphate of an abasic site
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
pyrimidine dimer-specific base excision repair pathway
-
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
-
moving a DNA base extrahelical opposite the target site that induces a conformational change to facilitate catalysis
-
?
DNA + H2O
?
-
the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
-
-
?
DNA + H2O
?
5'-GCTCGGCTICGGACCGAG-3'. Endonuclease V is an inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine
-
-
?
DNA + H2O
?
endonuclease V recognizes deoxyinosine and cleaves the second phosphodiester bond on the 3' side of the deaminated base lesion in damaged DNA. The enzyme possesses specific endonuclease activity for the deoxyinosine-containing DNA strand
-
-
?
DNA + H2O
?
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
-
?
DNA + H2O
?
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
-
?
DNA + H2O
?
the enzyme binds A:TT loops with higher affinity than undamaged DNA
-
-
?
DNA + H2O
?
-
the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
10fold lower activity than for single-stranded circular DNA, relaxed plasmid DNA, exposure to UV light or sodium bisulfite, to pH 5.2 or osmium tetroxide renders duplex DNA 7fold more active, best substrate is uracil containing DNA from Bacillus subtilis
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
removal of 3'deoxytermini
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
-
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
predominant release of a beta-elimination product rather than a hydrolytic product
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
-
supercoiled pBR322-DNA
-
?
RNA-DNA hybrid + H2O
?
-
the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA
-
-
?
RNA-DNA hybrid + H2O
?
the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA. The enzyme cleaves an RNA substrate containing inosine in a position corresponding to a biologically important site for deamination in the Gabra-3 transcript of the GABAA neurotransmitter. Further, the enzyme specifically incises transfer RNAs with inosine in the wobble position
-
-
?
single-stranded RNA + H2O
?
5'-CUGACUICGGAUCAGGGCC-3'. The enzyme is most active towards single-stranded RNA but is much less active towards other substrates
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single-stranded RNA + H2O
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in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
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single-stranded RNA + H2O
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in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
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additional information
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the enzyme shows affinity for but does not cleave branched DNA substrates like 5'-flap, 3'-flap, pseudo-Y, fork, 3-way junction, and Holliday junction
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additional information
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endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. But Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity and non-specific 5'-exonuclease activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Ca2+
protein binding, D43, E89, D110, and H214 have been identified as active site residues that are involved in metal coordination
Mg2+
activity is stimulated by the presence of Mg2+ or Mn2+ in the reaction buffer, with an optimum at 1 mM Mg2+
Mg2+
a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal
Mg2+
DNA cleavage, D43, E89, D110, and H214 have been identified as active site residues that are involved in metal coordination
Mg2+
contains one Mg2+ ion in the active site, which is required for activity
Mn2+
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highest cleavage activity for deoxyuridine-containing or mismatch-containing DNA at 2 mM
Mn2+
activity is stimulated by the presence of Mg2+ or Mn2+ in the reaction buffer, with an optimum at 1 mM Mg2+
Mn2+
a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal
Mn2+
in the presence of Mn2+, 3'-exonuclease activity is pronounced in wild type and mutant enzymes E89D, D110C, H214C, H214E, and H214D, while reduced activity is detected in D110A, D110H, and D110E
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
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50% inhibition at 25 mM, inhibition of formation of acid-soluble products
ATP
1 mM ATP almost completely inhibits hEndoV activity. hEndoV cleavage is inhibited by normal intracellular ATP concentrations. The ATP stores inside a cell do not overlay stress granules and it is suggest that hEndoV is redistributed to stress granules as a strategy to create a local environment low in ATP to permit hEndoV activity
Hg2+
Tequatrovirus T4
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50% inhibition at 0.0006 mM, inhibition of both DNA glycosylase and apurinic nicking activities, binding capability not reduced
Mn2+
at pH 8.5, a Mn2+ concentration of 2.5 mM and higher inhibits activity
additional information
Tequatrovirus T4
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an oligonucleotide duplex containing a 2'-fluorinated sugar moiety at the cyclobutane pyrimidine dimer (CPD) site inhibits the T4 Endo V reaction by stabilizing the covalent enzyme-DNA complex
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NaCl
activity is suppressed by high NaCl concentration. When adding 500 mM NaCl in the cleavage reaction, the cleavage efficiency of the enzyme is reduced to be approximately 50%. At NaCl concentrations over 800 mM, only slight endonuclease activity remains
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyadenylate-binding protein C1
the association between polyadenylate-binding protein C1 and hEndoV is RNA dependent. Polyadenylate-binding protein stimulates hEndoV activity and affinity for inosine-containing RNA. Upon cellular stress, polyadenylate-binding protein C1 relocates to cytoplasmic stress granules
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additional information
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high pH, metal cofactor Mn2+, using excess enzyme, and/or solvents such as dimethyl sulfoxide and betaine, lead to cleavage of most mismatched DNA base pairs
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additional information
high pH, metal cofactor Mn2+, using excess enzyme, and/or solvents such as dimethyl sulfoxide and betaine, lead to cleavage of most mismatched DNA base pairs
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