3.1.21.7: deoxyribonuclease V
This is an abbreviated version!
For detailed information about deoxyribonuclease V, go to the full flat file.
Word Map on EC 3.1.21.7
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3.1.21.7
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nick
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deaminate
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phosphodiester
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beta-polymerase
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deoxyinosine-containing
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3\'-hydroxyl
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proofreading
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biotechnology
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analysis
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molecular biology
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drug development
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medicine
- 3.1.21.7
- nick
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deaminate
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phosphodiester
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beta-polymerase
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deoxyinosine-containing
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3\'-hydroxyl
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proofreading
- biotechnology
- analysis
- molecular biology
- drug development
- medicine
Reaction
endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate =
Synonyms
AGTendoV, deoxyinosine 3' endonuclease, Deoxyinosine 3'endonuclease, DNase V, EC 3.1.22.3, endo V, endodeoxyribonuclease V, endonuclease V, EndoV, Escherichia coli endodeoxyribonuclease V, nfi, PF0987, PfuEndoV, T4 endonuclease V, T4 UV endonuclease, Tb10.6k15.3890
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Natural Substrates Products
Natural Substrates Products on EC 3.1.21.7 - deoxyribonuclease V
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REACTION DIAGRAM
deoxyinosine-containing deoxyoligonucleotide + H2O
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the enzyme is involved in damaged DNA repair
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RNA + H2O
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the enzyme also cleaves inosine-containing RNA strands
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single-stranded circular DNA + H2O
linearized single-stranded DNA
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10fold more activity than for duplex DNA
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5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
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cleavage of both denatured and native eukaryotic DNA
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
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also nicks duplex DNA exposed to OsO4, x-rays or acid, does not act upon undamaged DNA or irradiated single-stranded DNA
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
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cleaves deoxyinosine-containing DNA, urea residues-containing DNA, apurinic sites, base mismatches, insertion/deletion mismatches, flaps and pseudo-Y structures
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
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active at apurinic/apyrimidinic sites, UV light induced damages, adducts of 7-bromomethylbenz(a)anthracene, uracil-containing duplex DNA
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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two distinct activities: pyrimidine dimer glycosylase and apurinic-apyrimidinic endonuclease, beta-elimination of the 3'-phosphate of an abasic site
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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pyrimidine dimer-specific base excision repair pathway
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DNA + H2O
5'-phosphoryltermini DNA + 3'-hydroxyltermini DNA
Tequatrovirus T4
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moving a DNA base extrahelical opposite the target site that induces a conformational change to facilitate catalysis
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the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
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DNA + H2O
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5'-GCTCGGCTICGGACCGAG-3'. Endonuclease V is an inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine
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DNA + H2O
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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
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DNA + H2O
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endonuclease V is an important enzyme for repairing deoxyinosine in DNA
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DNA + H2O
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endonuclease V is an important enzyme for repairing deoxyinosine in DNA
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DNA + H2O
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the enzyme binds A:TT loops with higher affinity than undamaged DNA
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DNA + H2O
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the enzyme cleaves the second phosphodiester bond 3' to deoxyinosine
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nicked circular DNA + linearized DNA
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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
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
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removal of 3'deoxytermini
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
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predominant release of a beta-elimination product rather than a hydrolytic product
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
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supercoiled pBR322-DNA
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
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supercoiled pBR322-DNA
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double-stranded plasmid DNA + H2O
nicked circular DNA + linearized DNA
Tequatrovirus T4
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supercoiled pBR322-DNA
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the enzyme specifically cleaves the RNA strand of RNA-DNA hybrids. The enzyme is specific for inosine in RNA
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RNA-DNA hybrid + H2O
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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
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5'-CUGACUICGGAUCAGGGCC-3'. The enzyme is most active towards single-stranded RNA but is much less active towards other substrates
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single-stranded RNA + H2O
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in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
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single-stranded RNA + H2O
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in prokaryotes, endonuclease V (EndoV) can recognize and cleave inosine-containing DNA. In contrast, mammalian EndoVs preferentially cleave inosine-containing RNA, suggesting a role in RNA metabolism for the eukaryotic members of this protein family
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the enzyme shows affinity for but does not cleave branched DNA substrates like 5'-flap, 3'-flap, pseudo-Y, fork, 3-way junction, and Holliday junction
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additional information
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endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. But Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity and non-specific 5'-exonuclease activity
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