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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

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 Hydrolases
         3.1 Acting on ester bonds
             3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
                3.1.21.7 deoxyribonuclease V

Engineering

Engineering on EC 3.1.21.7 - deoxyribonuclease V

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D35A
-
inactive
D201N
the mutant enzyme has comparable RNase activity as wild-type enzyme
D52A
inactive
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
V29I
the mutant enzyme has comparable RNase activity as wild-type enzyme
Y91A
the mutant has lost its affinity for branched DNA substrates
D52A
mutant enzyme totally loses the inosine-RNA incision activity
D35A
inactive mutant 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
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
K121N
Tequatrovirus T4
-
decreased affinity for nontarget DNA
K86N
Tequatrovirus T4
-
decreased affinity for nontarget DNA
Q15R
Tequatrovirus T4
-
limited processive nicking activity
R117N
Tequatrovirus T4
-
limited processive nickin activity
R3Q
Tequatrovirus T4
-
greatly decreased DNA binding ability
A123I
-
levels of oxanosine and uridine cleavage are reduced by more than 90%
A138I
-
mutation reduces level of T/I cleavage by 10%
A86M
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
D110A
little cleavage activity
D43C
no more than 10% cleavage activity
D43E
no more than 10% cleavage activity
D43H
no more than 10% cleavage activity
E89A
about 20-30% cleavage activity
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%
G184V
-
mutation reduces the level of inosine and xanthosine cleavage
G83V
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
H116T
-
DNA and Mn2+ binding defective enzyme mutant
H125A
H214A
tolerant of mutation without impacting activity
H214C
tolerant of mutation without impacting activity
H214D
H214E
K139A
-
mutation reduces level of T/I cleavage by 10%
K139Q
-
mutation reduces level of T/I cleavage by 10%
K139R
-
mutation reduces level of T/I cleavage by 10%
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
Q20A
-
DNA and Mn2+ binding defective enzyme mutant
R118A
R205K
R211A
R211K
R88K
mismatch cleavage activity similar to the wild-type enzyme
R88Q
mismatch cleavage activity similar to the wild-type enzyme
R99Q
-
fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage
V137A
-
mutation reduces level of T/I cleavage by 10%
additional information