3.1.21.2: deoxyribonuclease IV
This is an abbreviated version!
For detailed information about deoxyribonuclease IV, go to the full flat file.
Word Map on EC 3.1.21.2
-
3.1.21.2
-
exonuclease
-
ape1
-
glycosylase
-
abasic
-
strand
-
endonucleases
-
single-stranded
-
nick
-
uracil
-
duplex
-
phosphodiester
-
uracil-dna
-
methanesulfonate
-
3'-blocking
-
8-oxoguanine
-
3'-phosphatase
-
depurinated
-
deoxyribose
-
3\'-hydroxyl
-
xrcc1
-
diesterase
-
incise
-
site-containing
-
base-excision
-
endonucleolytic
-
8-oxog
-
soxrs
-
ap-site
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5'-deoxyribose
-
cross-complementing
-
non-ltr
-
repair-deficient
-
exoiiis
-
5'-phosphorylated
-
uracil-containing
-
non-long
-
3'-phosphoglycolate
-
asp148glu
-
analysis
-
pharmacology
- 3.1.21.2
-
exonuclease
- ape1
- glycosylase
-
abasic
- strand
- endonucleases
-
single-stranded
- nick
- uracil
- duplex
-
phosphodiester
-
uracil-dna
- methanesulfonate
-
3'-blocking
- 8-oxoguanine
-
3'-phosphatase
-
depurinated
- deoxyribose
-
3\'-hydroxyl
- xrcc1
- diesterase
-
incise
-
site-containing
-
base-excision
-
endonucleolytic
-
8-oxog
-
soxrs
-
ap-site
-
5'-deoxyribose
-
cross-complementing
-
non-ltr
-
repair-deficient
- exoiiis
-
5'-phosphorylated
-
uracil-containing
-
non-long
-
3'-phosphoglycolate
-
asp148glu
- analysis
- pharmacology
Reaction
Endonucleolytic cleavage of ssDNA at apurinic/apyrimidinic sites to 5'-phosphooligonucleotide end-products =
Synonyms
apurinic/apyrimidinic endonuclease, coliphage T4 endonuclease II, deoxriboendonuclease, DNA-adenine-transferase, E. coli endonuclease IV, EC 3.1.4.30, End, Endo IV, endodeoxyribonuclease IV, EndoII, EndoIV, endonuclease II, endonuclease IV, exonuclease III, More, MtbEndo IV, MtbNfo, MtbXthA, Nfo, nuclease, endodeoxyribo-oder redoxyendonuclease, Rv0670, Sco4631, ScoA3McrA, T4 endonuclease IV, TthNfo, type IV methyl-dependent restriction endonuclease
ECTree
3.1.21.2 deoxyribonuclease IVAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 3.1.21.2 - deoxyribonuclease IV
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Co2+
CoCl2
-
can substitute for MgCl2, optimal concentration: 0.01 M, activity 27% higher than at optimal MgCl2 concentration
KCl
Mg2+
MgCl2
-
absolute requirement, no activity in absence, optimal concentration: 0.01 M
Mn2+
Zn2+
additional information
Ca2+
the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity
Co2+
the enzyme exhibits a non-linear dependence in the presence of Co2+. The AP site cleavage activity increases from 0.1 to 0.5 mM and then rapidly decreases from 0.5 to 10 mM CoCl2
KCl
the enzyme requires high ionic strength, 200 mM KCl
Mg2+
the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity
Mg2+
the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Under pH 7.6 optimal cation concentrations for MtbXthA-catalyzed activities are 2 mM MgCl2 and/or 0.5 mM MnCl2
Mn2+
the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Depending on pH, the enzyme requires different concentrations of divalent cations: 0.5 mM MnCl2 at pH 7.6 and 10 mM at pH 6.5. It exhibits a non-linear dependence in the presence of Mn2+. The AP site cleavage activity increases from 0.1 to 0.5 mM and then rapidly decreases from 0.5 to 10 mM MnCl2. 10 mM MnCl2 is optimal
Mn2+
the enzyme requires the presence of Mg2+ and, to lesser extent, Ca2+ and Mn2+ for the DNA repair activity. Depending on pH, the enzyme requires different concentrations of divalent cations: 0.5 mM MnCl2 at pH 7.6 and 10 mM at pH 6.5. Under pH 7.6 optimal cation concentrations for MtbXthA-catalyzed activities are 2 mM MgCl2 and/or 0.5 mM MnCl2
Mn2+
contains Mn2+, the enzyme with Mn2+ and Zn2+ is more active than with only Zn2+
additional information
-
the enzyme shows no absolute requirement for divalent cations, no effect by Ca2+
additional information
the enzyme shows metal ion independent 3'->5' exonuclease activity
additional information
-
the enzyme shows metal ion independent 3'->5' exonuclease activity
additional information
the presence of Zn2+, Fe2+ and Ni2+ does not significantly stimulate AP endonuclease activity
additional information
the presence of Zn2+, Fe2+ and Ni2+ does not significantly stimulate AP endonuclease activity
additional information
-
the presence of Zn2+, Fe2+ and Ni2+ does not significantly stimulate AP endonuclease activity
