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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
-
-
?
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
?
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
-
-
?
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
?
-
-
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+
-
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
-
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
-
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
-
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
-
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
-
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
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Liver Neoplasms, Experimental
Interaction of mammalian deoxyribonuclease V, a double strand 3' to 5' and 5' to 3' exonuclease, with deoxyribonucleic acid polymerase-beta from the Novikoff hepatoma.
Neoplasms
Switching base preferences of mismatch cleavage in endonuclease V: an improved method for scanning point mutations.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
49-mer oligonucleotide
Tequatrovirus T4
-
mutant Q15R and R117N enzymes, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.005
49-mer oligonucleotide
Tequatrovirus T4
-
wild type enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.013
49-mer oligonucleotide
Tequatrovirus T4
-
mutant K121N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.024
49-mer oligonucleotide
Tequatrovirus T4
-
mutant K86N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000333
49-mer oligonucleotide
Tequatrovirus T4
-
mutant K121N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.00167
49-mer oligonucleotide
Tequatrovirus T4
-
mutant R117N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.005
49-mer oligonucleotide
Tequatrovirus T4
-
mutant Q15R enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.00667
49-mer oligonucleotide
Tequatrovirus T4
-
mutant K86N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.0117
49-mer oligonucleotide
Tequatrovirus T4
-
wild type enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
between pH 6.0 and pH 9.0, the enzyme exhibits more than 86% cleavage efficiency
7 - 8.8
pH 7.0: about 45% of maximal activity, pH 8.8: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
a moderate reaction temperature is used for the biochemical studies, because of the melting temperature of the DNA duplex substrates (Tm = 67ºC)
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 100
60°C: about 45% of maximal activity, 100°C: about 70% of maximal activity
70 - 80
70°C: about 50% of maximal activity, 80°C: about 35% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
hEndoV both have a cytoplasmic localization. It relocates to cytoplasmic stress granules in cultured human cells upon exposure to various toxic agents. This is a mechanism for the cell to regulate hEndoV activity
brenda
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
brenda
-
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
brenda
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
brenda
-
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
brenda
the enzyme relocates to cytoplasmic stress granules in cultured human cells upon exposure to various toxic agents. This is a mechanism for the cell to regulate hEndoV activity
-
brenda
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
brenda
-
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
-
brenda
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
brenda
-
the enzyme is mainly cytosolic yet upon nutritional stress it redistributes and accumulates in stress granules colocalizing with the DEAD-box helicase TbDhh1
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
this DNA repair enzyme is also involved in RNA metabolism
physiological function
additional information
-
the deoxyinosine-containing heteroduplex is added to a purified system consisting of soluble endonuclease V fusion protein, DNA polymerase I, and DNA ligase, along with the four deoxynucleoside triphosphates. The three proteins alone are sufficient to process the dI lesion efficiently, and the 3'-exonuclease activity of DNA polymerase I is sufficient to remove the dI lesion in this minimum reconstituted assay, overview
malfunction
RNAi-mediated depletion of TbEndoV results in moderate growth defects in procyclic cells while the two EndoV alleles can be readily knocked out in bloodstream forms
malfunction
RNAi-mediated depletion of TbEndoV results in moderate growth defects in procyclic cells while the two EndoV alleles can be readily knocked out in bloodstream forms. The enzyme has an important role in RNA metabolism in procyclic forms of the parasite
malfunction
-
RNAi-mediated depletion of TbEndoV results in moderate growth defects in procyclic cells while the two EndoV alleles can be readily knocked out in bloodstream forms
-
malfunction
-
RNAi-mediated depletion of TbEndoV results in moderate growth defects in procyclic cells while the two EndoV alleles can be readily knocked out in bloodstream forms. The enzyme has an important role in RNA metabolism in procyclic forms of the parasite
-
physiological function
-
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
physiological function
DNA repair enzyme, may also be involved in RNA metabolism
physiological function
the DNA repair enzyme recognizes and cleaves DNA at deaminated adenine lesions (hypoxanthine) In addition, the enzyme cleaves DNA containing various helical distortions such as loops, hairpins, and flaps
physiological function
the enzyme is involved in damaged DNA repair
physiological function
adenine bases in DNA, RNA, and nucleotides are deaminated during normal metabolism via hydrolytic and nitrosative reactions. In RNA, the deaminated product inosine is resolved by human endonuclease V
physiological function
DNA polymerase I proofreading exonuclease activity is required for endonuclease V repair pathway
physiological function
endonuclease V has an important role in RNA metabolism in procyclic forms of the parasite
physiological function
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
physiological function
EndoV is a single-conformation and single-binding-site protein that switches between three distinct DNA scanning modes, each with a clear range of activation energy barriers. It is involved in the repair pathways for removing DNA damage
physiological function
-
the enzyme plays important roles in DNA repair. This method exhibits high sensitivity and desirable selectivity
physiological function
-
endonuclease V has an important role in RNA metabolism in procyclic forms of the parasite
-
physiological function
-
DNA polymerase I proofreading exonuclease activity is required for endonuclease V repair pathway
-
physiological function
-
EndoV is a single-conformation and single-binding-site protein that switches between three distinct DNA scanning modes, each with a clear range of activation energy barriers. It is involved in the repair pathways for removing DNA damage
-
physiological function
-
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
Show AA Sequence and Transmembrane Helices (8025 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
16000
Tequatrovirus T4
-
gel filtration sedimentation equilibrium technique in the presence of 100 mM KCl
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method at 25 °C, 2.4 A crystal structure
sitting drop vapor diffusion method, using 19% (w/v) PEG 3350, 0.2 M sodium formate, 0.1 M Tris-HCl pH 7.5 or 1.4 M ammonium sulfate, 0.2 M sodium acetate, 0.1 M Tris-HCl pH 7.5
2.75 A resolution, complexed with a duplex DNA substrate, adenine base complementary to the 5'-side of the thymine dimer is completely flipped out of the DNA duplex
Tequatrovirus T4
-
EndoV in complex with a hypoxanthine lesion substrate and with product DNA, hanging drop vapour diffusion method, in 6-12% (w/v) MPEG 2k in 200 mM imidazole-matate buffer, pH 5.8-7.4
in complex with DNA containing one nucleotide A:TT loop, vapor diffusion method, using 15% (w/v) polyethylene glycol 400 and 100 mM MES, pH 6.3
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D201N
the mutant enzyme has comparable RNase activity as wild-type enzyme
H141Y
the mutant enzyme is catalytically impaired, it generates less than one-third of the cleavage product produced by wild-type, suggesting that individuals homozygous for H141Y may be predisposed to disease
K114R
the mutant enzyme has comparable RNase activity as wild-type enzyme
R112Q
the mutant enzyme has comparable RNase activity as wild-type enzyme
C78T
Tequatrovirus T4
-
100 times more activity in the presence Hg2+ or Ag+ at concentrations they are required to inhibit the wild type enzyme
E23D
Tequatrovirus T4
-
altered affinities for pyrrolidine- and tetrahydrofuran-residues or reduced apurinic sites
E23Q
F59L
Tequatrovirus T4
-
remains in the monomeric state independent of salt concentration, alteration of target site location
F60L
Tequatrovirus T4
-
remains in the monomeric state independent of salt concentration, alteration of target site location
A123I
-
levels of oxanosine and uridine cleavage are reduced by more than 90%
A86M
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
D43A
F46A
-
mutation reduces the levels of oxanosine and uridine cleavage to less than 40%
F87A
-
mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates
G111V
-
levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 40%
G113V
-
levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 50%
G121V
-
levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 10%
G127V
-
levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 70%
G41V
G83V
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
H125A
H214D
H214E
I81A
L85V
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
P207A
P209A
P79A
-
mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates
P82A
R118A
R205K
R211A
R211K
R88E
R99Q
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
Y80A
Y80F
Y80H
additional information
E23Q
Tequatrovirus T4
-
altered affinities for a pyrrolidine- and tetrahydrofuran residues or reduced apurinic sites
G41V
-
mutation reduces the levels of oxanosine and uridine cleavage to less than 40%
H214D
little change in substrate specificity or DNA cleavage kinetics
I81A
-
mutant essentially maintains wild-type level activity towards inosine, xanthosine and uridine substrates, 40% less active towards oxanosine substrates
P82A
-
mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates, 70% less active towards oxanosine substrates
R88E
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
Y80A
-
mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates
Y80A
the mutant is severely compromised in its ability to bind to DNA base lesions and the corresponding nicked product
Y80F
-
mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates, partially active on G/U substrate
Y80F
the mutant is similar to the wild type EndoV in its ability to bind to DNA base lesions and the corresponding nicked product
Y80H
-
mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates
Y80H
the mutant is severely compromised in its ability to bind to DNA base lesions and the corresponding nicked product
additional information
-
the deoxyinosine-containing heteroduplex is added to a purified system consisting of soluble endonuclease V fusion protein, DNA polymerase I, and DNA ligase, along with the four deoxynucleoside triphosphates. The three proteins alone are sufficient to process the dI lesion efficiently, and the 3'-exonuclease activity of DNA polymerase I is sufficient to remove the dI lesion in this minimum reconstituted assay, overview. Reconstitution of endonuclease V-mediated repair in vitro
additional information
-
construction of enzyme mutants defective in DNA binding and Mn2+ as a metal cofactor. The majority of the binding defective mutants show varying degrees of non-specific activities
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
30% remaining activity for deoxyinosine-containing DNA above, less than 10% remaining mismatch repair activity above
288775
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
the enzyme withstands 100°C for 120 min without significant loss of its activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, HiTrap heparin column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a modified version of Escherichia coli ER 2566 (ER2566DELTAnfiDELTArnhB) where the endogenous nfi and rnhB genes have been inactivated by transformation with the kanamycin-deletion cassettes derived from the JW5547-1 (nfi::kan) and JW0178-1 (rnhB::kan) strains. For crystallisation, a site specific (D52A) truncated (residues 1-250) mutant of mEndoV is fused to His/MBP in pETM41 is expressed in BL21 CodonPlus(DE3)-RIPL Escherichia coli cells
expression in Escherichia coli
HEK 293T cells are transiently transfected with a vector expressing GFP-hEndoVwt
overexpression in Escherichia coli
the MBP-TbEndoV protein is overexpressed in the Escherichia coli TB1 strain
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
Tequatrovirus T4
-
determination of the minimum value of triplet energies for a photosensitizer to produce thymine cyclobutane dimer in DNA
biotechnology
-
method of linear amplification of DNA, allows 100fold amplification of target molecules
drug development
Tequatrovirus T4
-
investigated as a chemopreventive agent of nonmelanoma skin cancer
medicine
Tequatrovirus T4
-
in xeroderma pigmentosum patients, topical application of liposome-encapsulated T4 endonuclease V reduces the incidence of basal cell carcinomas by 30% and of actinic keratoses by more than 68%
molecular biology
-
application to DNA shuffling. Random DNA fragmentation by endonuclease V is a handy and reproducible method and can be used instead of fragmentation by DNase I, which is technically problematic due to decreasing shuffling efficiency
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nyaga, S.G.; Dodson, M.L.; Lloyd, R.S.
Role of specific amino acid residues in T4 endonuclease V that alter nontarget DNA binding
Biochemistry
36
4080-4088
1997
Tequatrovirus T4
brenda
McCullough, A.K.; Dodson, M.L.; Schrer, O.D.; Lloyd, R.S.
The role pf base flipping in damge recognition and catalysis by nT4 endonuclease V
J. Biol. Chem.
272
27210-27217
1997
Tequatrovirus T4
brenda
Vassylyev, D.G.; Kashiwagi, T.; Mikami, Y.; Ariyoshi, M.; Iwai, S.; Ohtsuka, E.; Morikawa, K.
Atomic model of a pyrmidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition
Cell
83
773-782
1995
Tequatrovirus T4
brenda
McCullough, A.K.; Schrer, O.; Verdine, G.L.; Lloyd, R.S.
Structural determinants for specific recognition by T4 endonuclease V
J. Biol. Chem.
271
32147-32152
1996
Tequatrovirus T4
brenda
Yao, M.; Kow, Y.W.
Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA
J. Biol. Chem.
272
30774-30779
1997
Escherichia coli
brenda
Latham, K.A.; Rajendran, S.; Carmical, J.R.; Lee, J.C.; Lloyd, R.S.
T4 endonuclease V exists in solution as a monomer and binds to target sites as a monomer
Biochim. Biophys. Acta
1292
324-334
1996
Tequatrovirus T4
brenda
Latham, K.A.; Lloyd, R.S.
delta-Eliminiation by T4 endonuclease V at a thymine dimer site requires a secondary binding event and amino acid Glu-23
Biochemistry
34
8796-8803
1995
Tequatrovirus T4
brenda
Dodson, M.L.; Schrockk III, R.D.; Lloyd, R.S.
Evidence for an imino intermediate in the T4 endonuclease V reaction
Biochemistry
32
8284-8290
1993
Tequatrovirus T4
brenda
Sibghat-Ullah; Sancar, A.
In vitro characterization of repair synthesis initiated by T4 endonuclease V on a synthetic DNA substrate
Indian J. Biochem. Biophys.
29
227-230
1992
Tequatrovirus T4
brenda
Nickell, C.; Lloyd, R.S.
Mutations in endonuclease V that affect both protein-protein association and target site location
Biochemistry
30
8638-8648
1991
Tequatrovirus T4
brenda
Prince, M.A.; Friedman, B.; Gruskin, E.A.; Schrock III, R.D.; Lloyd, R.S.
Selective metal binding to Cys-78 within endonuclease V cause an inhibition of catalytic aactivities without altering nontarget and target DNA binding
J. Biol. Chem.
266
10686-10693
1991
Tequatrovirus T4
brenda
Morikawa, K.; Matsumoto, O.; Tsujimoto, M.; Katayanagi, K.; Ariyoshi, M.; Doi, T.; Ikehara, M.; Inaoka, T.; Ohtsuka, E.
X-ray structure of T4 endonuclease V: An excision repair enzyme specific for a pyrimidine dimer
Science
256
523-526
1992
Tequatrovirus T4
brenda
Kim, J.; Linn, S.
The mechanism of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites
Nucleic Acids Res.
16
1135-1141
1988
Tequatrovirus T4
brenda
Mosbaugh, D.W.; Linn, S.
Excision repair and DNA synthesis with a combination of HeLa DNA polymerase beta and DNase V
J. Biol. Chem.
258
108-118
1983
Homo sapiens
brenda
Demple, B.; Linn, S.
On the recognition and cleavage mechanism of Escherichia coli endodeoxyribonuclease V, a possible DNA repair enzyme
J. Biol. Chem.
257
2848-2855
1982
Escherichia coli
brenda
Demple, B.; Gates III, F.T.; Linn, S.
Purification and properties of Escherichia coli endodeoxyribonuclease V
Methods Enzymol.
65
224-231
1980
Escherichia coli
brenda
Wang, E.G.; Furth, J.J.
Mammalian endonuclease, DNase V. Purification and properties of enzyme of calf thymus
J. Biol. Chem.
252
116-124
1977
Bos taurus
brenda
Gates III, F.T.; Linn, S.
Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays
J. Biol. Chem.
252
2802-2807
1977
Escherichia coli
brenda
Kanugula, S.; Pauly, G.T.; Moschel, R.C.; Pegg, A.E.
A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities
Proc. Natl. Acad. Sci. USA
102
3617-3622
2005
Ferroplasma acidarmanus
brenda
Feng, H.; Dong, L.; Klutz, A.M.; Aghaebrahim, N.; Cao, W.
Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V
Biochemistry
44
11486-11495
2005
Thermotoga maritima
brenda
Feng, H.; Klutz, A.; Cao, W.
Active site plasticity of endonuclease V from Salmonella typhimurium
Biochemistry
44
675-683
2005
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Miyazaki, K.
Random DNA fragmentation with enonuclease V: application to DNA shuffling
Nucleic Acids Res.
30
e139
2002
Escherichia coli
brenda
Hitchcock, T.M.; Gao, H.; Cao, W.
Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V
Nucleic Acids Res.
32
4071-4080
2004
Salmonella sp.
brenda
Doi, Y.; Katafuchi, A.; Fujiwara, Y.; Hitomi, K.; Tainer, J.A.; Ide, H.; Iwai, S.
Synthesis and characterization of oligonucleotides containing 2'-fluorinated thymidine glycol as inhibitors of the endonuclease III reaction
Nucleic Acids Res.
34
1540-1551
2006
Tequatrovirus T4
brenda
Turner, D.J.; Pingle, M.R.; Barany, F.
Harnessing asymmetrical substrate recognition by thermostable EndoV to achieve balanced linear amplification in multiplexed SNP typing
Biochem. Cell Biol.
84
232-242
2006
Thermotoga maritima
brenda
Feng, H.; Dong, L.; Cao, W.
Catalytic Mechanism of Endonuclease V: A Catalytic and Regulatory Two-Metal Model
Biochemistry
45
10251-10259
2006
Thermotoga maritima (Q9X2H9)
brenda
Lin, J.; Gao, H.; Schallhorn, K.A.; Harris, R.M.; Cao, W.; Ke, P.C.
Lesion Recognition and Cleavage by Endonuclease V: A Single-Molecule Study
Biochemistry
46
7132-7137
2007
Thermotoga maritima (Q9X2H9)
brenda
Wright, T.I.; Spencer, J.M.; Flowers, F.P.
Chemoprevention of nonmelanoma skin cancer
J. Am. Acad. Dermatol.
54; 933-46
quiz 947-50
2006
Tequatrovirus T4
brenda
Lhiaubet-Vallet, V.; Cuquerella, M.C.; Castell, J.V.; Bosca, F.; Miranda, M.A.
Triplet excited fluoroquinolones as mediators for thymine cyclobutane dimer formation in DNA
J. Phys. Chem. B
111
7409-7414
2007
Tequatrovirus T4
brenda
Gao, H.; Huang, J.; Barany, F.; Cao, W.
Switching base preferences of mismatch cleavage in endonuclease V: an improved method for scanning point mutations
Nucleic Acids Res.
35
e2/1-e2/6
2007
Thermotoga maritima (Q9X2H9)
-
brenda
Jiang, Y.; Rabbi, M.; Kim, M.; Ke, C.; Lee, W.; Clark, R.L.; Mieczkowski, P.A.; Marszalek, P.E.
UVA generates pyrimidine dimers in DNA directly
Biophys. J.
96
1151-1158
2009
Tequatrovirus T4
brenda
Dong, K.K.; Damaghi, N.; Picart, S.D.; Markova, N.G.; Obayashi, K.; Okano, Y.; Masaki, H.; Grether-Beck, S.; Krutmann, J.; Smiles, K.A.; Yarosh, D.B.
UV-induced DNA damage initiates release of MMP-1 in human skin
Exp. Dermatol.
17
1037-1044
2008
Tequatrovirus T4
brenda
Cafardi, J.A.; Elmets, C.A.
T4 endonuclease V: review and application to dermatology
Expert. Opin. Biol. Ther.
8
829-838
2008
Tequatrovirus T4
brenda
Majorek, K.A.; Bujnicki, J.M.
Modeling of Escherichia coli Endonuclease V structure in complex with DNA
J. Mol. Model.
15
173-182
2009
Escherichia coli
brenda
Dalhus, B.; Arvai, A.S.; Rosnes, I.; Olsen, O.E.; Backe, P.H.; Alseth, I.; Gao, H.; Cao, W.; Tainer, J.A.; Bjoras, M.
Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair
Nat. Struct. Mol. Biol.
16
138-143
2009
Thermotoga maritima (Q9X2H9)
brenda
Lee, C.; Yang, Y.; Goodman, S.; Yu, Y.; Lin, S.; Kao, J.; Tsai, K.; Fang, W.
Endonuclease V-mediated deoxyinosine excision repair in vitro
DNA Repair
9
1073-1079
2010
Escherichia coli
brenda
Mi, R.; Abole, A.; Cao, W.
Dissecting endonuclease and exonuclease activities in endonuclease V from Thermotoga maritima
Nucleic Acids Res.
39
536-544
2011
Thermotoga maritima
brenda
Kiyonari, S.; Egashira, Y.; Ishino, S.; Ishino, Y.
Biochemical characterization of endonuclease V from the hyperthermophilic archaeon, Pyrococcus furiosus
J. Biochem.
155
325-333
2014
Pyrococcus furiosus (Q8U263), Pyrococcus furiosus
brenda
Zhang, Z.; Hao, Z.; Wang, Z.; Li, Q.; Xie, W.
Structure of human endonuclease V as an inosine-specific ribonuclease
Acta Crystallogr. Sect. D
70
2286-2294
2014
Homo sapiens (Q8N8Q3)
brenda
Baumann, T.; Arndt, K.; Mueller, K.
Directional cloning of DNA fragments using deoxyinosine-containing oligonucleotides and endonuclease V
BMC Biotechnol.
13
81
2013
Escherichia coli, Thermotoga maritima
brenda
Vik, E.S.; Nawaz, M.S.; Strom Andersen, P.; Fladeby, C.; Bjoras, M.; Dalhus, B.; Alseth, I.
Endonuclease V cleaves at inosines in RNA
Nat. Commun.
4
2271
2013
Escherichia coli, Homo sapiens (Q8N8Q3)
brenda
Fladeby, C.; Vik, E.S.; Laerdahl, J.K.; Gran Neurauter, C.; Heggelund, J.E.; Thorgaard, E.; Strom-Andersen, P.; Bjoras, M.; Dalhus, B.; Alseth, I.
The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures
PLoS ONE
7
e47466
2012
Homo sapiens (Q8N8Q3)
brenda
Rosnes, I.; Rowe, A.D.; Vik, E.S.; Forstrom, R.J.; Alseth, I.; Bjoras, M.; Dalhus, B.
Structural basis of DNA loop recognition by endonuclease V
Structure
21
257-265
2013
Thermotoga maritima (Q9X2H9)
brenda
Ishino, S.; Makita, N.; Shiraishi, M.; Yamagami, T.; Ishino, Y.
EndoQ and EndoV work individually for damaged DNA base repair in Pyrococcus furiosus
Biochimie
118
264-269
2015
Pyrococcus furiosus (Q8U263)
brenda
Wang, W.; Peng, F.; Li, W.; Huang, Y.; Nie, Z.; Yao, S.
A dual enzymatic amplified strategy for the detection of endonuclease v activity
Anal. Methods
7
8453-8458
2015
Escherichia coli
-
brenda
Su, K.Y.; Lin, L.I.; Goodman, S.D.; Yen, R.S.; Wu, C.Y.; Chang, W.C.; Yang, Y.C.; Cheng, W.C.; Fang, W.H.
DNA polymerase I proofreading exonuclease activity is required for endonuclease V repair pathway both in vitro and in vivo
DNA Repair
64
59-67
2018
Escherichia coli (P68739), Escherichia coli, Escherichia coli K12 (P68739)
brenda
Kim, J.; Tohashi, K.; Iwai, S.; Kuraoka, I.
Inosine-specific ribonuclease activity of natural variants of human endonuclease V
FEBS Lett.
590
4354-4360
2016
Homo sapiens (Q8N8Q3)
-
brenda
Wang, Y.; Zhang, L.; Zhu, X.; Li, Y.; Shi, H.; Oger, P.; Yang, Z.
Biochemical characterization of a thermostable endonuclease V from the hyperthermophilic euryarchaeon Thermococcus barophilus Ch5
Int. J. Biol. Macromol.
117
17-24
2018
Thermococcus barophilus (A0A0S1X9V3), Thermococcus barophilus, Thermococcus barophilus Ch5 (A0A0S1X9V3)
brenda
Nawaz, M.S.; Vik, E.S.; Berges, N.; Fladeby, C.; Bjoras, M.; Dalhus, B.; Alseth, I.
Regulation of human endonuclease V activity and relocalization to cytoplasmic stress granules
J. Biol. Chem.
291
21786-21801
2016
Homo sapiens (Q8N8Q3)
brenda
Ahmadi, A.; Rosnes, I.; Blicher, P.; Diekmann, R.; Schuettpelz, M.; Glette, K.; Torresen, J.; Bjoras, M.; Dalhus, B.; Rowe, A.D.
Breaking the speed limit with multimode fast scanning of DNA by endonuclease V
Nat. Commun.
9
5381
2018
Thermotoga maritima (Q9X2H9), Thermotoga maritima ATCC 43589 (Q9X2H9)
brenda
Zhang, Z.; Jia, Q.; Zhou, C.; Xie, W.
Crystal structure of E. coli endonuclease V, an essential enzyme for deamination repair
Sci. Rep.
5
12754
2015
Escherichia coli (B7MIY4), Escherichia coli O45:K1/S88/ExPEC (B7MIY4), Escherichia coli O45:K1/S88 (B7MIY4)
brenda
Nawaz, M.S.; Vik, E.S.; Ronander, M.E.; Solvoll, A.M.; Blicher, P.; Bjoras, M.; Alseth, I.; Dalhus, B.
Crystal structure and MD simulation of mouse EndoV reveal wedge motif plasticity in this inosine-specific endonuclease
Sci. Rep.
6
24979
2016
Mus musculus (Q8C9A2)
brenda
Garcia-Caballero, D.; Perez-Moreno, G.; Estevez, A.M.; Ruiz-Perez, L.M.; Vidal, A.E.; Gonzalez-Pacanowska, D.
Insights into the role of endonuclease V in RNA metabolism in Trypanosoma brucei
Sci. Rep.
7
8505
2017
Trypanosoma brucei (Q38AS1), Trypanosoma brucei brucei (Q38AS1), Trypanosoma brucei 927 (Q38AS1), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38AS1)
brenda
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