Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Im, E.K.; Han, Y.S.; Chung, J.H.
    Functional changes in a novel uracil-DNA glycosylase determined by mutational analyses (2008), Mikrobiologiia, 77, 644-650.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.27 expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.27 D150E site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
3.2.2.27 D150E displays reduced activity of about 70% of the wild type value Methanocaldococcus jannaschii
3.2.2.27 D150W site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity Methanocaldococcus jannaschii
3.2.2.27 D150W completely lacks DNA glycosylase activity Methanocaldococcus jannaschii
3.2.2.27 E132K site-directed mutagenesis, a mutation in the HhH motif with a lysine residue equivalent to Lys120 in endonuclease III leading to conversion of the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an AP site. Mutant E132K catalyzes a beta-elimination reaction at the AP site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex Methanocaldococcus jannaschii
3.2.2.27 E132K mutation converts the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an apurinic/apyrimidinic site. The mutant catalyzes a beta-elimination reaction at the apurinic/apyrimidinic site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex Methanocaldococcus jannaschii
3.2.2.27 Y152E site-directed mutagenesis, the mutant shows unaltered enzyme activity compared to the wild-type enzyme Methanocaldococcus jannaschii
3.2.2.27 Y152E retains unchanged levels of uracil-DNA glycosylase activity Methanocaldococcus jannaschii
3.2.2.27 Y152N site-directed mutagenesis, the mutant shows unaltered enzyme activity compared to the wild-type enzyme Methanocaldococcus jannaschii
3.2.2.27 Y152N retains unchanged levels of uracil-DNA glycosylase activity Methanocaldococcus jannaschii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.27 24000
-
x * 24000, SDS-PAGE Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.27 Methanocaldococcus jannaschii
-
-
-
3.2.2.27 Methanocaldococcus jannaschii Q58829
-
-
3.2.2.27 Methanocaldococcus jannaschii DSM 2661 Q58829
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.27
-
Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.27 uracil-mismatched double-stranded oligonucleotide + H2O oligonucleotide duplex containing a U:T mispair Methanocaldococcus jannaschii uracil + double-stranded oligonucleotide with abasic site
-
?
3.2.2.27 uracil-mismatched double-stranded oligonucleotide + H2O oligonucleotide duplex containing a U:T mispair Methanocaldococcus jannaschii DSM 2661 uracil + double-stranded oligonucleotide with abasic site
-
?

Subunits

EC Number Subunits Comment Organism
3.2.2.27 ? x * 24000, SDS-PAGE Methanocaldococcus jannaschii
3.2.2.27 More UDG contains a helix-hairpin-helix motif and Gly/Pro rich loop in the GPD region important for catalytic activity Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.2.2.27 MjUDG
-
Methanocaldococcus jannaschii
3.2.2.27 UDG
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.27 50
-
assay at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.27 6
-
assay at Methanocaldococcus jannaschii