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
-
deaminate
-
phosphodiester
-
beta-polymerase
-
deoxyinosine-containing
-
3\'-hydroxyl
-
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
ECTree
3.1.21.7 deoxyribonuclease VAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.1.21.7 - deoxyribonuclease V
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Mg2+
Mn2+
Ca2+
protein binding, D43, E89, D110, and H214 have been identified as active site residues that are involved in metal coordination
Mg2+
activity is stimulated by the presence of Mg2+ or Mn2+ in the reaction buffer, with an optimum at 1 mM Mg2+
Mg2+
a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal
Mg2+
DNA cleavage, D43, E89, D110, and H214 have been identified as active site residues that are involved in metal coordination
Mg2+
contains one Mg2+ ion in the active site, which is required for activity
Mn2+
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highest cleavage activity for deoxyuridine-containing or mismatch-containing DNA at 2 mM
Mn2+
activity is stimulated by the presence of Mg2+ or Mn2+ in the reaction buffer, with an optimum at 1 mM Mg2+
Mn2+
a divalent metal ion is required for the enzyme to cleave DNA, Mn2+ (1 mM) and Mg2+ (1 mM) are optimal
Mn2+
in the presence of Mn2+, 3'-exonuclease activity is pronounced in wild type and mutant enzymes E89D, D110C, H214C, H214E, and H214D, while reduced activity is detected in D110A, D110H, and D110E
