DNA glycosylase
From Proteopedia
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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]] }} | {{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]] }} | ||
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'''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.<br /> | '''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.<br /> | ||
Revision as of 10:07, 1 December 2015
Function
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
