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Literature summary extracted from

  • Maiti, A.; Morgan, M.T.; Drohat, A.C.
    Role of two strictly conserved residues in nucleotide flipping and N-glycosylic bond cleavage by human thymine DNA glycosylase (2009), J. Biol. Chem., 284, 36680-36688.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.29 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
3.2.2.29 N140A/R275L site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview Homo sapiens
3.2.2.29 R275A site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview Homo sapiens
3.2.2.29 R275L site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, overview Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.29 additional information
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 additional information pre-steady-state kinetics, and minimal kinetic mechanism for TDG, single turnover kinetics, detailed, overview Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.29 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

EC Number Organism UniProt Comment Textmining
3.2.2.29 Homo sapiens Q13569
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.29 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 ?
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 ?
3.2.2.29 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

EC Number Synonyms Comment Organism
3.2.2.29 More the enzyme is a member of the uracil DNA glycosylase, UDG, superfamily Homo sapiens
3.2.2.29 TDG
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 Homo sapiens
3.2.2.29 thymine DNA glycosylase
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 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.29 22
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 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.29 7.5
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 assay at Homo sapiens