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Literature summary extracted from

  • Matsubara, M.; Tanaka, T.; Terato, H.; Ohmae, E.; Izumi, S.; Katayanagi, K.; Ide, H.
    Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase (2004), Nucleic Acids Res., 32, 5291-5302.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.27 expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.27 F98H site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 F98L site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 G87A site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 H239L site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 H239N site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 N163D site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens
3.2.2.27 N85A site-directed mutagenesis, the mutant shows reduced activity with uracil, 5-hydroxyuracil, 5-hydroxymethyluracil, and 5-formyluracil compared to the wild-type enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.27 additional information
-
 additional information kinetics of mutant enzymes, overview Homo sapiens
3.2.2.27 0.0000022
-
 uracil-mismatched double-stranded DNA with U-G mismatch pH 7.5, 37°C, wild-type enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.27 5-formyluracil-mismatched double-stranded DNA + H2O Homo sapiens
-
 5-formyluracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 5-hydroxymethyluracil-mismatched double-stranded DNA + H2O Homo sapiens
-
 5-hydroxymethyluracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 5-hydroxyuracil-mismatched double-stranded DNA + H2O Homo sapiens
-
 5-hydroxyuracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 uracil-mismatched double-stranded DNA + H2O Homo sapiens
-
 uracil + double-stranded DNA with abasic site
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.27 Homo sapiens Q53HV7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.27 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.27 5-formyluracil-mismatched double-stranded DNA + H2O
-
 Homo sapiens 5-formyluracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
-
 Homo sapiens 5-hydroxymethyluracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 5-hydroxyuracil-mismatched double-stranded DNA + H2O
-
 Homo sapiens 5-hydroxyuracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 additional information substrate specificity, the enzyme is not active with other oxidized pyrimidines such as 5-hydroxycytosine, 5-formylcytosine and thymine glycol, and intact pyrimidines such as thymine and cytosine. Mutational analysis of the catalytic and damage-recognition mechanism of hSMUG1, overview Homo sapiens ?
-
 ?
3.2.2.27 uracil-mismatched double-stranded DNA + H2O
-
 Homo sapiens uracil + double-stranded DNA with abasic site
-
 ?
3.2.2.27 uracil-mismatched double-stranded DNA with U-G mismatch + H2O
-
 Homo sapiens uracil + double-stranded DNA with abasic site
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.27 More three-dimensional structure and molecular modelling Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.2.27 single-strand selective monofunctional uracil-DNA glycosylase
-
 Homo sapiens
3.2.2.27 SMUG1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.27 37
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.2.27 0.014
-
 uracil-mismatched double-stranded DNA with U-G mismatch pH 7.5, 37°C, wild-type enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.27 7.5
-
 assay at Homo sapiens