Protein Variants | Comment | Organism |
---|---|---|
N140A | site-directed mutagenesis, the mutant variant binds substrate DNA with the same tight affinity as wild-type TDG, but it has no detectable base excision activity for a G:T substrate, and its excision rate is vastly diminished for G:U, G:FU, i.e. fluorouridine, and G:BrU, i.e. bromodeoxyuridine, substrates. Altered kinetics compared to the wild-type enzyme, overview | Homo sapiens |
N140A/R275L | site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview | Homo sapiens |
R275A | site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview | Homo sapiens |
R275L | site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state kinetics, and minimal kinetic mechanism for TDG, single turnover kinetics, detailed, overview | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | TDG promotes genomic integrity by excising thymine from mutagenic G:T mismatches arising by deamination of 5-methylcytosine, and follow-on base excision repair enzymes restore a G:C pair. TDG cleaves the N-glycosylic bond of dT and some other nucleotides, including 5-substituted 2'-deoxyuridine analogues, once they are flipped from the helix into its active site. All of the DNA glycosylases employ nucleotide flipping to extrude the target nucleotide from the helix and gain access to the damaged base and the scissile N-glycosylic bond | ? | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q13569 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TDG promotes genomic integrity by excising thymine from mutagenic G:T mismatches arising by deamination of 5-methylcytosine, and follow-on base excision repair enzymes restore a G:C pair. TDG cleaves the N-glycosylic bond of dT and some other nucleotides, including 5-substituted 2'-deoxyuridine analogues, once they are flipped from the helix into its active site. All of the DNA glycosylases employ nucleotide flipping to extrude the target nucleotide from the helix and gain access to the damaged base and the scissile N-glycosylic bond | Homo sapiens | ? | - |
? | |
additional information | TDG cleaves the N-glycosylic bond of dT and some other nucleotides, including 5-substituted 2'-deoxyuridine analogues, once they are flipped from the helix into its active site. Residue Asn140, in motif 138GINPG142, is implicated in the chemical step, does not contribute substantially to substrate binding, and residue Arg275 in nucleotide flipping, Arg275 penetrates the DNA minor groove, filling the void created by nucleotide flipping, active site structure, overview. DNA glycosylases employ nucleotide flipping to extrude the target nucleotide from the helix and gain access to the damaged base and the scissile N-glycosylic bond. The enzyme can also remove 5-halogenated uracils, 5-fluorouracil, 5-chlorouracil, 5-bromouracil, and 5-iodouracil, many other 5-substituted uracils, N4-ethenocytosine, hypoxanthine, and other damaged bases, but not with substrate analogueG:2'-deoxy-2'-fluoroarabinouridine, substrate binding structure and kinetics, overview | Homo sapiens | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
More | the enzyme is a member of the uracil DNA glycosylase, UDG, superfamily | Homo sapiens |
TDG | - |
Homo sapiens |
thymine DNA glycosylase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |