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Literature summary extracted from

  • Henry, R.A.; Mancuso, P.; Kuo, Y.M.; Tricarico, R.; Tini, M.; Cole, P.A.; Bellacosa, A.; Andrews, A.J.
    Interaction with the DNA repair protein thymine DNA glycosylase regulates histone acetylation by p300 (2016), Biochemistry, 55, 6766-6775 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.29 expressed in MEF cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.29 P65A the mutant shows impaired activity compared to the wild type enzyme 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 thymine-mismatched double-stranded DNA + H2O Homo sapiens
-
 thymine + double-stranded DNA with abasic site
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.29 Homo sapiens Q13569
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.29 HiTrap Q column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.29 thymine-mismatched double-stranded DNA + H2O
-
 Homo sapiens thymine + double-stranded DNA with abasic site
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.2.29 TDG
-
 Homo sapiens
3.2.2.29 thymine DNA glycosylase
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.2.29 malfunction the enzyme interacts with the CH3 domain of histone acetyltransferase p300 to allosterically promote p300 activity to specific lysines on histone H3 (K18 and K23). The absence of the enzyme in mouse embryonic fibroblasts leads to a reduction in the rate of histone acetylation Homo sapiens
3.2.2.29 physiological function when enzyme concentrations approach those of histones, the enzyme acts as a competitive inhibitor of p300 histone acetylation Homo sapiens