DNA glycosylase

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[[Image:1akz.png|left|200px|thumb|Crystal Structure of DNA glycosylate, [[1akz]]]]
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{{STRUCTURE_3fsp| PDB=3fsp | SIZE=400| SCENE= |right|CAPTION=Adenine DNA glycosylate complex with DNA, Fe4-S4 cluster, phosphoric acid esther and Ca+2 ion [[3fsp]] }}
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{{STRUCTURE_3fsp| PDB=3fsp | SIZE=350| SCENE= |right|CAPTION=Adenine DNA glycosylate complex with DNA, Fe4-S4 cluster, phosphoric acid esther and Ca+2 ion [[3fsp]] }}

Revision as of 10:06, 1 December 2015

Template:STRUCTURE 3fsp











DNA glycosylase (DG) are enzymes which remove damaged DNA bases by flipping them out of the double helix followed by their cleavage. Monofunctional DG have only glycosylase activity; bifunctional DG also act as lysates; ADG, UDG, TDG remove adenine, uracil, thymine from DNA.

  • Adenine DNA glycosylase is also called MutY.
  • Thymine DNA glycosylase removes thymine moieties from mismatched G/T, C/T and T/T.
  • Smug1 is a single-strand selective monofunctional UDG.
  • 8-oxoguanine DNA glycosylase recognize oxidized bases.
  • Human 8-oxoguanine GD is named hOgg1. See details on Ogg1 in 8-Oxoguanine Glycosylase.
  • Methyladenine DNA glycosylase recognize methylated adenine; for details see Alka1.
  • Formamidopyrimidine DG (FPG) or MutM or Fapy-DNA glycosylase removes oxidized purines from damaged DNA. More about FPG in
  • Fpg Nei Protein Family
  • Fpg Nei Protein Superfamily.

3D Structures of DNA glycosylate

Updated on 01-December-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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