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Information on EC 3.1.21.7 - deoxyribonuclease V
for references in articles please use BRENDA:EC3.1.21.7
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
3.1.21.7 deoxyribonuclease V
IUBMB Comments
Previously classified erroneously as EC 3.1.22.3.
The enzyme appears in viruses and cellular organisms
- 3.1.21.7
- nick
-
deaminate
-
phosphodiester
-
beta-polymerase
-
deoxyinosine-containing
-
3\'-hydroxyl
-
proofreading
- biotechnology
- analysis
- molecular biology
- drug development
- medicine
Reaction Schemes
showendonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate
Synonyms
endo v, dnase v, deoxyinosine 3' endonuclease, agtendov, pfuendov, deoxyinosine 3'endonuclease, escherichia coli endodeoxyribonuclease v, more
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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
AK6
aurora kinase
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
SiRe_0242
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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
12-mer oligonucleotide + H2O
hydrolyzed DNA
-
Substrates: double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
Products: -
Products: -
?
18-mer RNA oligonucleotide containing inosine + H2O
?
Substrates: -
Products: -
Products: -
?
21-mer ssRNA oligonucleotide containing inosine at residue 11 + H2O
?
Substrates: -
Products: -
Products: -
?
30-mer DNA/RNA containing inosine hybrid + H2O
?
Substrates: -
Products: -
Products: -
?
34-mer oligonucleotide + H2O
fragments of 34mer-oligonucleotide
-
Substrates: oligonucleotide duplex containing a fluorine atom at the 2' position of the 5' component of the cyclobutane pyrimidine dimer
Products: -
Products: -
?
48-mer oligonucleotide + H2O
24-mer oligonucleotide
-
Substrates: double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
Products: 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
Products: 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
-
Substrates: 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
Products: delta-elimination reaction
Products: delta-elimination reaction
?
deoxyinosine-containing RNA + H2O
?
Substrates: (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
Products: -
Products: -
?
deoxyinosine-containing single-stranded DNA + H2O
?
Substrates: precursor activity of DNA repair
Products: -
Products: -
?
DNA + H2O
3-alpha,beta-unsaturated aldehyde + 5'-phosphate DNA-termini
-
Substrates: abasic lyase activity
Products: -
Products: -
?
dsDNA containing deoxyinosine + H2O
?
Substrates: 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
Products: -
Products: -
?
single-stranded circular DNA + H2O
linearized single-stranded DNA
-
Substrates: 10fold more activity than for duplex DNA
Products: -
Products: -
?
49-mer oligonucleotide + H2O
hydrolysed DNA
-
Substrates: also possesses abasic lyase activity
Products: -
Products: -
?
49-mer oligonucleotide + H2O
hydrolysed DNA
-
Substrates: double-stranded, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
Products: -
Products: -
?
deoxyinosine-containing deoxyoligonucleotide + H2O
?
Substrates: the enzyme is involved in damaged DNA repair
Products: -
Products: -
?
deoxyinosine-containing deoxyoligonucleotide + H2O
?
Substrates: the enzyme hydrolyzes the second phosphodiester bond 3' from deoxyinosine
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: cleavage of both denatured and native eukaryotic DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: also nicks duplex DNA exposed to OsO4, x-rays or acid, does not act upon undamaged DNA or irradiated single-stranded DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: cleaves deoxyinosine-containing DNA, urea residues-containing DNA, apurinic sites, base mismatches, insertion/deletion mismatches, flaps and pseudo-Y structures
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: active at apurinic/apyrimidinic sites, UV light induced damages, adducts of 7-bromomethylbenz(a)anthracene, uracil-containing duplex DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: pyrimidine dimer-specific
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: two distinct activities: pyrimidine dimer glycosylase and apurinic-apyrimidinic endonuclease, beta-elimination of the 3'-phosphate of an abasic site
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: pyrimidine dimer-specific base excision repair pathway
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: moving a DNA base extrahelical opposite the target site that induces a conformational change to facilitate catalysis
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: endonuclease V repairs UV-induced cyclobutane pyrimidine dimers in DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Substrates: EndoV hydrolyzes the second phosphodiester bond 3' of a deaminated base using Mg2+ as a cofactor
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme nicks uracil-containing DNA at the seond or third phosphodiester bond 3' to uracil sites
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
Products: -
Products: -
?
DNA + H2O
?
Substrates: dI-containing heteroduplex DNAs are constructed, in which the dI resided in a disrupted restriction endonuclease recognition sites of bacteriophage M13mp18 DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Substrates: dI-containing heteroduplex DNAs are constructed, in which the dI resided in a disrupted restriction endonuclease recognition sites of bacteriophage M13mp18 DNA
Products: -
Products: -
?
DNA + H2O
?
Escherichia coli O45:K1/S88
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Escherichia coli O45:K1/S88/ExPEC
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Substrates: 5'-GCTCGGCTICGGACCGAG-3'. Endonuclease V is an inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine
Products: -
Products: -
?
DNA + H2O
?
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Substrates: endonuclease V is an important enzyme for repairing deoxyinosine in DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: endonuclease V is an important enzyme for repairing deoxyinosine in DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: the enzyme exhibits a higher affinity for binding to deoxyinosine-containing DNA than normal DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: the enzyme binds A:TT loops with higher affinity than undamaged DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
Products: -
Products: -
?
DNA + H2O
?
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Substrates: 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
Products: -
Products: -
?
DNA + H2O
hydrolysed DNA
-
Substrates: supercoiled circular DNA
Products: -
Products: -
?
DNA + H2O
hydrolysed DNA
Substrates: hydrolysis of the second phosphodiester bond 3' from a deaminated base lesion including inosine, xanthosine, oxanosine and uridine
Products: -
Products: -
?
DNA + H2O
hydrolysed DNA
Substrates: cleavage of deaminated bases at the second phosphodiester bond 3' downstream to a lesion
Products: -
Products: -
?
DNA + H2O
hydrolysed DNA
-
Substrates: cleavage of unmodified duplex DNA
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: 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
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: removal of 3'deoxytermini
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: -
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: predominant release of a beta-elimination product rather than a hydrolytic product
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: supercoiled pBR322-DNA
Products: -
Products: -
?
double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: -
Products: -
Products: -
?
dsDNA containing hypoxanthine + H2O
?
Substrates: -
Products: -
Products: -
?
dsDNA containing hypoxanthine + H2O
?
Substrates: -
Products: -
Products: -
?
RNA + H2O
?
Substrates: the enzyme cleaves RNA with inosine but not DNA
Products: -
Products: -
?
RNA + H2O
?
Substrates: the enzyme is active on RNA substrates containing one or several inosines. It does not cleave at inosines in DNA
Products: -
Products: -
?
RNA + H2O
?
Substrates: the enzyme also cleaves inosine-containing RNA strands
Products: -
Products: -
?
RNA-DNA hybrid + H2O
?
-
Substrates: the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA
Products: -
Products: -
?
RNA-DNA hybrid + H2O
?
Substrates: 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
Products: -
Products: -
?
single-stranded RNA + H2O
?
Substrates: 5'-CUGACUICGGAUCAGGGCC-3'. The enzyme is most active towards single-stranded RNA but is much less active towards other substrates
Products: -
Products: -
?
single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
?
single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
?
single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
?
single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
?
ssDNA containing hypoxanthine + H2O
?
Substrates: -
Products: -
Products: -
?
ssDNA containing hypoxanthine + H2O
?
Substrates: -
Products: -
Products: -
?
ssRNA rI + H2O
?
Substrates: 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
Products: -
Products: -
?
ssRNA rI + H2O
?
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: Endo V protein cleaves the second and third phosphodiester bonds, 3' to inosine in single-strand RNA. EndoV does not exhibit any nuclease activity on the ssDNA and dsDNA substrates tested or dsRNA-containing I : U or I : C pairings
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: a dual enzymatic amplified strategy for the detection of EndoV activity based on a nicking enzyme and a template independent polymerase is developed
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: EndoV displays similar efficiencies for cleaving hypoxanthine:T and hypoxanthine:G-containing dsDNA and about 38% of these efficiencies for cleaving hypoxanthine:A containing dsDNA
Products: -
Products: -
-
additional information
?
-
Substrates: EndoV displays similar efficiencies for cleaving hypoxanthine:T and hypoxanthine:G-containing dsDNA and about 38% of these efficiencies for cleaving hypoxanthine:A containing dsDNA
Products: -
Products: -
-
additional information
?
-
-
Substrates: endonuclease V detects apurinic/apyrimidinic site base paired with adenine and cyclobutane pyrimidine dimers in UV-damaged DNA
Products: -
Products: -
?
additional information
?
-
-
Substrates: enhanced cyclobutane pyrimidine dimer repair in UV-irradiated keratinocytes by T4 endonuclease V reduces the induction of matrix metalloproteinase-1 mRNA
Products: -
Products: -
?
additional information
?
-
Substrates: EndoV has a strong preference for RNA over DNA and selectively acts on inosine, but not 1-methylinosine
Products: -
Products: -
-
additional information
?
-
Substrates: poor substrates: 30-mer dsRNA oligonucleotide containing inosine, 30-mer DNA oligonucleotide containing deoxyinosine, 30-mer DNA containing deoxyinosine/RNA, 30-mer dsDNA oligonucleotide containing deoxyinosine
Products: -
Products: -
-
additional information
?
-
-
Substrates: 3'-exonuclease activity in endonuclease V might be preferentially triggered by the specific cleavage event at the inosine site
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleavage of 50-labeled inosine- and non-inosine-containing substrates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
deoxyinosine-containing deoxyoligonucleotide + H2O
?
Substrates: the enzyme is involved in damaged DNA repair
Products: -
Products: -
?
RNA + H2O
?
Substrates: the enzyme also cleaves inosine-containing RNA strands
Products: -
Products: -
?
single-stranded circular DNA + H2O
linearized single-stranded DNA
-
Substrates: 10fold more activity than for duplex DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: cleavage of both denatured and native eukaryotic DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: also nicks duplex DNA exposed to OsO4, x-rays or acid, does not act upon undamaged DNA or irradiated single-stranded DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: cleaves deoxyinosine-containing DNA, urea residues-containing DNA, apurinic sites, base mismatches, insertion/deletion mismatches, flaps and pseudo-Y structures
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: active at apurinic/apyrimidinic sites, UV light induced damages, adducts of 7-bromomethylbenz(a)anthracene, uracil-containing duplex DNA
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: pyrimidine dimer-specific
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: two distinct activities: pyrimidine dimer glycosylase and apurinic-apyrimidinic endonuclease, beta-elimination of the 3'-phosphate of an abasic site
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: pyrimidine dimer-specific base excision repair pathway
Products: -
Products: -
?
DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
-
Substrates: moving a DNA base extrahelical opposite the target site that induces a conformational change to facilitate catalysis
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
Products: -
Products: -
?
DNA + H2O
?
Substrates: 5'-GCTCGGCTICGGACCGAG-3'. Endonuclease V is an inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine
Products: -
Products: -
?
DNA + H2O
?
Substrates: 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
Products: -
Products: -
?
DNA + H2O
?
Substrates: endonuclease V is an important enzyme for repairing deoxyinosine in DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: endonuclease V is an important enzyme for repairing deoxyinosine in DNA
Products: -
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DNA + H2O
?
Substrates: the enzyme binds A:TT loops with higher affinity than undamaged DNA
Products: -
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DNA + H2O
?
-
Substrates: the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
Products: -
Products: -
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: 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
Products: -
Products: -
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: removal of 3'deoxytermini
Products: -
Products: -
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: -
Products: -
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: predominant release of a beta-elimination product rather than a hydrolytic product
Products: -
Products: -
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
-
Substrates: supercoiled pBR322-DNA
Products: -
Products: -
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RNA-DNA hybrid + H2O
?
-
Substrates: the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA
Products: -
Products: -
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RNA-DNA hybrid + H2O
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Substrates: 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
Products: -
Products: -
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single-stranded RNA + H2O
?
Substrates: 5'-CUGACUICGGAUCAGGGCC-3'. The enzyme is most active towards single-stranded RNA but is much less active towards other substrates
Products: -
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single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
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single-stranded RNA + H2O
?
Substrates: 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
Products: -
Products: -
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additional information
?
-
Substrates: 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
Products: -
Products: -
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additional information
?
-
-
Substrates: 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
Products: -
Products: -
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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+
activity is dependent on a divalent metal ion, among which Mg2+ is optimal
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+
-
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
-
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
-
mutant Q15R and R117N enzymes, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.005
49-mer oligonucleotide
-
wild type enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.013
49-mer oligonucleotide
-
mutant K121N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.024
49-mer oligonucleotide
-
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
0.035
18-mer RNA oligonucleotide containing inosine
pH 7.5, 65°C
-
0.0063
30-mer DNA/RNA containing inosine hybrid
pH 7.5, 65°C
-
0.000333
49-mer oligonucleotide
-
mutant K121N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.00167
49-mer oligonucleotide
-
mutant R117N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.005
49-mer oligonucleotide
-
mutant Q15R enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.00667
49-mer oligonucleotide
-
mutant K86N enzyme, double-stranded substrate, containing a site-specific duplex cis-syn cyclobutane pyrimidine dimer
-
0.0117
49-mer oligonucleotide
-
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
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
-
171808, 288772, 288773, 288774, 288776, 288777, 288778, 288779, 288780, 288781, 288782, 288783, 666506, 680338, 681597, 691338, 692218, 692249
-
-
brenda
three complete transcripts exist with open reading frames encoding 282 (Q8N8Q3), 308 and 309 amino acids
SwissProt
brenda
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
-
metabolism
this DNA repair enzyme is also involved in RNA metabolism
metabolism
activation energy for cleaving hypoxanthine-containing ssDNA is 9.6 kcal/mol
metabolism
-
activation energy for cleaving hypoxanthine-containing ssDNA is 9.6 kcal/mol
-
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
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 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
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
physiological function
-
the enzyme plays important roles in DNA repair. This method exhibits high sensitivity and desirable selectivity
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
aurora kinase isoform AK6 contains a C?terminal endonuclease V domain. AK6 interacts with DNA repair proteins and Sir2a, involved in regulating microtubular assembly
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 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
-
endonuclease V is an important enzyme for repairing deoxyinosine in DNA
-
physiological function
-
aurora kinase isoform AK6 contains a C?terminal endonuclease V domain. AK6 interacts with DNA repair proteins and Sir2a, involved in regulating microtubular assembly
-
Show AA Sequence and Transmembrane Helices (4253 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
16000
-
gel filtration sedimentation equilibrium technique in the presence of 100 mM KCl
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
transcript variants hENDOV 282, hENDOV 308 and hENDOV 309 comprise all exons encoding the conserved catalytic core. hENDOV 308 and hENDOV 309 transcripts are more abundant than hENDOV 282 transcripts in immortalized cell lines, but not in primary cells. hENDOV 309 binds inosine-containing RNA with stronger affinity than the other isoforms. Mass spectrometry analyses identified peptides corresponding to the hENDOV 309 isoform only
?
x * 31000, calculated from sequence, x * 57000, SDS-PAGE of recombinant His-tagged GFP-fused protein
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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
-
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
Y100A
mutation bears a mutation in substrate recognition sites, mutant is catalytically impaired
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
D189A
residue D189 is involved in both DNA cleavage and DNA binding, mutant displays about 35% of wild-type activity
D38A
residue D38 is essential for catalysis, but has no role in DNA binding. Mutation abolishes almost completely the cleavage activity
Y41A
residue Y41 is involved in both DNA cleavage and DNA binding, mutant displays about 70% of wild-type activity
D189A
-
residue D189 is involved in both DNA cleavage and DNA binding, mutant displays about 35% of wild-type activity
-
D38A
-
residue D38 is essential for catalysis, but has no role in DNA binding. Mutation abolishes almost completely the cleavage activity
-
Y41A
-
residue Y41 is involved in both DNA cleavage and DNA binding, mutant displays about 70% of wild-type activity
-
C78T
-
100 times more activity in the presence Hg2+ or Ag+ at concentrations they are required to inhibit the wild type enzyme
E23D
-
altered affinities for pyrrolidine- and tetrahydrofuran-residues or reduced apurinic sites
E23Q
F59L
-
remains in the monomeric state independent of salt concentration, alteration of target site location
F60L
-
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
-
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
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
recombinant His-tagged GFP-fused protein, purified via two-step affinity purification
recombinant protein, purified via heparin, hydroxyapatite and HiTrap SP HP columns
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNA expression of AK6 is increased upon UV-C irradiation in wild-type and also in the AK6 over-expressing transformants
mRNA expression of AK6 is increased upon UV-C irradiation in wild-type and also in the AK6 over-expressing transformants
mRNA expression of AK6 is increased upon UV-C irradiation in wild-type and also in the AK6 over-expressing transformants
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
method of linear amplification of DNA, allows 100fold amplification of target molecules
drug development
-
investigated as a chemopreventive agent of nonmelanoma skin cancer
medicine
-
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
analysis
-
determination of the minimum value of triplet energies for a photosensitizer to produce thymine cyclobutane dimer in DNA
analysis
method to sequence the dI modification site in DNA, which utilizes endonuclease V-dependent deamination repair to specifically label the modification site with biotin-14-dATP. The method allows the affinity enrichment of dI-bearing DNA for sequencing
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
molecular biology
method for construction of DNA libraries based on the use of PCR primers containing a single deoxyinosine (I) residue near their 5' end. Treatment of the PCR products with endonuclease V generates 3' overhangs with customized lengths and sequences, which can be ligated accurately and efficiently with other fragments having exactly complementary overhangs. The method is cost-effective and scalable
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Tequatrovirus T4
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Tequatrovirus T4
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Tequatrovirus T4
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Tequatrovirus T4
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Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays
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Escherichia coli
brenda
Kanugula, S.; Pauly, G.T.; Moschel, R.C.; Pegg, A.E.
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Thermotoga maritima
brenda
Feng, H.; Klutz, A.; Cao, W.
Active site plasticity of endonuclease V from Salmonella typhimurium
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Salmonella enterica subsp. enterica serovar Typhimurium
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Miyazaki, K.
Random DNA fragmentation with enonuclease V: application to DNA shuffling
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Escherichia coli
brenda
Hitchcock, T.M.; Gao, H.; Cao, W.
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brenda
Doi, Y.; Katafuchi, A.; Fujiwara, Y.; Hitomi, K.; Tainer, J.A.; Ide, H.; Iwai, S.
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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
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Thermotoga maritima
brenda
Feng, H.; Dong, L.; Cao, W.
Catalytic Mechanism of Endonuclease V: A Catalytic and Regulatory Two-Metal Model
Biochemistry
45
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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
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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
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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
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Thermotoga maritima (Q9X2H9)
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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
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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
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17
1037-1044
2008
Tequatrovirus T4
brenda
Cafardi, J.A.; Elmets, C.A.
T4 endonuclease V: review and application to dermatology
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8
829-838
2008
Tequatrovirus T4
brenda
Majorek, K.A.; Bujnicki, J.M.
Modeling of Escherichia coli Endonuclease V structure in complex with DNA
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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
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155
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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
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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.
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81
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Thermotoga maritima, Escherichia coli
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.
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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
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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.
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FEBS Lett.
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Homo sapiens (Q8N8Q3)
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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.
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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.
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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 (B7MIY4), Escherichia coli O45:K1/S88/ExPEC (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 927 (Q38AS1), Trypanosoma brucei brucei (Q38AS1), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38AS1)
brenda
Yamamoto, Y.; Terai, T.; Kumachi, S.; Nemoto, N.
In vitro construction of large-scale DNA libraries from fragments containing random regions using deoxyinosine-containing oligonucleotides and endonuclease V
ACS Comb. Sci.
22
165-171
2020
Escherichia coli (P68739)
brenda
Zheng, X.; Chen, D.; Zhao, Y.; Dai, X.; You, C.
Development of an endonuclease V-assisted analytical method for sequencing analysis of deoxyinosine in DNA
Anal. Chem.
94
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2022
Escherichia coli (P68739)
brenda
Shiraishi, M.; Hidaka, M.; Iwai, S.
Endonuclease V from the archaeon Thermococcus kodakarensis is an inosine-specific ribonuclease
Biosci. Biotechnol. Biochem.
86
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2022
Thermococcus kodakarensis (Q5JI47)
brenda
Biswas, P.; Ghosh, R.; Das, M.; Pal, S.; Dam, S.
Molecular characterization of EhAK6, an endonuclease V domain-containing aurora kinase protein from Entamoeba histolytica Protein-protein interaction, docking and functional aspect
Curr. Res. Biotechnol.
3
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2021
Entamoeba histolytica (C4LY26), Entamoeba histolytica ATCC 30459 (C4LY26)
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brenda
Endo, M.; Kim, J.I.; Shioi, N.A.; Iwai, S.; Kuraoka, I.
Arabidopsis thaliana endonuclease V is a ribonuclease specific for inosine-containing single-stranded RNA
Open Biol.
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Arabidopsis thaliana (F4JJL3)
brenda
Berges, N.; Nawaz, M.S.; Borresdatter Dahl, T.; Hagen, L.; Bjoras, M.; Laerdahl, J.K.; Alseth, I.
Complex alternative splicing of human Endonuclease V mRNA, but evidence for only a single protein isoform
PLoS ONE
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2019
Homo sapiens (Q8N8Q3)
brenda
Yin, Y.; Shi, J.; Zhang, L.; Liu, Q.; Gong, Y.; Oger, P.; Liu, X.
Biochemical and mutational studies of an endonuclease V from the hyperthermophilic crenarchaeon Sulfolobus islandicus REY15A
World J. Microbiol. Biotechnol.
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Saccharolobus islandicus (F0NDK4), Saccharolobus islandicus Rey15A (F0NDK4)
brenda
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