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Literature summary for 3.2.2.27 extracted from

  • Wibley J.E.; Waters T.R.; Haushalter K.; Verdine G.L.; Pearl L.H.
    Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1 (2003), Mol. Cell, 11, 1647-59.
    View publication on PubMed
Search for more literature for 3.2.2.27

Protein Variants

Protein Variants Comment Organism
additional information Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1 Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus SMUG1 is specialized for antimutational uracil excision in mammalian cells. Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1 ?
-
 ?
uracil-mismatched single-stranded DNA + H2O Mus musculus
-
 uracil + single-stranded DNA with abasic site
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q6P5C5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SMUG1 is specialized for antimutational uracil excision in mammalian cells. Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1 Mus musculus ?
-
 ?
additional information SMUG1 also excises the oxidation-damage product 5-hydroxymethyluracil, but like UNG is inactive against thymine, i.e. 5-methyluracil, displacement/replacement mechanism allowing SMUG1 to exclude thymine from its active site while accepting 5-hydroxymethyluracil, overview Mus musculus ?
-
 ?
uracil-mismatched single-stranded DNA + H2O
-
 Mus musculus uracil + single-stranded DNA with abasic site
-
 ?

Synonyms

Synonyms Comment Organism
SMUG1
-
 Mus musculus