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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

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 Hydrolases
         3.1 Acting on ester bonds
             3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
                3.1.21.2 deoxyribonuclease IV

Engineering

Engineering on EC 3.1.21.2 - deoxyribonuclease IV

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G149D
-
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities
H69A
-
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities. The crystal structure of Nfo-H69A mutant reveals the loss of one of the active site zinc atoms and rearrangements of the catalytic site, but no gross changes in the overall enzyme conformation
G149D
-
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities
-
H69A
-
site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities. The crystal structure of Nfo-H69A mutant reveals the loss of one of the active site zinc atoms and rearrangements of the catalytic site, but no gross changes in the overall enzyme conformation
-
H508A
E118A
Tequatrovirus T4
-
site-directed mutagenesis
S176N
Tequatrovirus T4
-
mutant enzyme retains cleavage activity (17.5% of that of wild-type Endo IV), but loses the polarized and restricted cleavage of a dCs tract. Escherichia coli cells expressing the intact Endo IV mutant enzyme are viable and, in contrast to wild-type Endo IV, the mutant enzyme does not show detrimental effect on the host cells
W88R
Tequatrovirus T4
-
mutant enzyme shows no enzymatic activity (less than 0.4% of that of wild-type Endo IV). Escherichia coli cells expressing the intact Endo IV mutant enzyme are viable and, in contrast to wild-type Endo IV, these mutant enzymes do not show detrimental effect on the host cells
additional information
-
analysis of enzyme activity in naturally occurring mutants of Escherichia coli compared to wild-type strain enzymes, overview