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

BRENDA support

Literature summary for 3.2.2.29 extracted from

  • Aziz, M.A.; Schupp, J.E.; Kinsella, T.J.
    Modulation of the activity of methyl binding domain protein 4 (MBD4/MED1) while processing iododeoxyuridine generated DNA mispairs (2009), Cancer Biol. Ther., 8, 1156-1163.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition of TDG activity on methylated G:IU mispairs by the methyl binding domain Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens thymine DNA glycosylase and methyl binding domain protein 4 act on G:IU, i.e. iododeoxyuridine, but not A:IU, mispairs and are functionally complementary to each other ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information thymine DNA glycosylase and methyl binding domain protein 4 act on G:IU, i.e. iododeoxyuridine, but not A:IU, mispairs and are functionally complementary to each other Homo sapiens ?
-
?
additional information IUdR is a thymidine analogue which has been used in the clinic as a radiosensitizer. Following active cell membrane transport, IUdR is sequentially phosphorylated to IdUTP which competes with thymidine, TdR, for DNA incorporation. G:IU mispair is a substrate for thymidine DNA glycosylase Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
TDG
-
Homo sapiens
thymine DNA glycosylase
-
Homo sapiens