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Literature summary for 3.2.2.27 extracted from

  • Mi, R.; Dong, L.; Kaulgud, T.; Hackett, K.W.; Dominy, B.N.; Cao, W.
    Insights from xanthine and uracil DNA glycosylase activities of bacterial and human SMUG1: switching SMUG1 to UDG (2009), J. Mol. Biol., 385, 761-778.
    View publication on PubMed
Search for more literature for 3.2.2.27

Cloned(Commentary)

Cloned (Comment) Organism
SMUG1, DNA and amino acid sequence determination and analysis Geobacter metallireducens
SMUG1, sequence comparison Homo sapiens

Protein Variants

Protein Variants Comment Organism
A214R site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview Geobacter metallireducens
G60Y site-directed mutagenesis, the mutation completely abolishes XDG and UDG activity, which is consistent with a modeled structure in which G60Y blocks the entry of either xanthine or uracil to the base binding pocket Geobacter metallireducens
G63P site-directed mutagenesis, the proline substitution at the G63 position switches the SMUG1 enzyme to an exclusive UDG with equal activity for all uracil-DNA base pairs Geobacter metallireducens
H210G site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview Geobacter metallireducens
H210M site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview Geobacter metallireducens
H210N site-directed mutagenesis, the mutant shows altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview Geobacter metallireducens
M57L site-directed mutagenesis, the mutation increases the flexibility of the motif 2 loop region and specifically A214, the mutant shows reduced catalytic activity and altered substrate specificity for cleavage of uracil-DNA base pairs in comparison to the wild-type enzyme, overview Geobacter metallireducens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substrate specificity, kinetic analysis Geobacter metallireducens

Organism

Organism UniProt Comment Textmining
Geobacter metallireducens Q39ZI0 SMUG1; SMUG1
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Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210 Q39ZI0 SMUG1; SMUG1
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Homo sapiens Q53HV7 SMUG1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15 Homo sapiens ?
-
 ?
additional information SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15, but is not active in excising hypoxanthine and oxanine from DNA Geobacter metallireducens ?
-
 ?
additional information SMUG1 is an uracil-DNA glycosylase, that also shows xanthine-DNA glycosylase activity, XDG, EC 3.2.2.15, but is not active in excising hypoxanthine and oxanine from DNA Geobacter metallireducens GS-15 / ATCC 53774 / DSM 7210 ?
-
 ?

Subunits

Subunits Comment Organism
More mutational analysis and molecular dynamics simulations of SMUG1 identify important structural determinants in conserved motifs 1 and 2 for XDG and UDG activities Geobacter metallireducens

Synonyms

Synonyms Comment Organism
More SMUG1 belongs to the family 3 of the UDG superfamily Geobacter metallireducens
More SMUG1 belongs to the family 3 of the UDG superfamily Homo sapiens
single-strand-selective monofunctional uracil DNA glycosylase
-
 Geobacter metallireducens
single-strand-selective monofunctional uracil DNA glycosylase
-
 Homo sapiens
SMUG1
-
 Geobacter metallireducens
SMUG1
-
 Homo sapiens