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Literature summary for 3.2.2.27 extracted from
- Structure and function in the uracil-DNA glycosylase superfamily (2000), Mutat. Res., 460, 165-181.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | ? | - |
? |  |
| additional information | Homo sapiens | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | ? | - |
? | |
| additional information | Human alphaherpesvirus 1 | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | ? | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | Escherichia coli | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | Homo sapiens | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | Human alphaherpesvirus 1 | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | uracil + double-stranded DNA with abasic site | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Human alphaherpesvirus 1 | P10186 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | Escherichia coli | ? | - |
? | |
| additional information | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | Homo sapiens | ? | - |
? | |
| additional information | family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family | Human alphaherpesvirus 1 | ? | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | Escherichia coli | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | Homo sapiens | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway | Human alphaherpesvirus 1 | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | substrate recognition by family-1 UDG, modelling, detailed overview | Human alphaherpesvirus 1 | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | substrate recognition by family-1 UDG, no activity against G-T mismatches or any of a range of other possible substrates, modelling, detailed overview | Homo sapiens | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched double-stranded DNA + H2O | the enzyme hydrolyses the N-glycosidic bond connecting the base to the deoxyribose sugar of the DNA backbone, releasing free uracil base and DNA containing an abasic site, as its products, substrate recognition by family-1 UDG, modelling, detailed overview | Escherichia coli | uracil + double-stranded DNA with abasic site | - |
? | |
| uracil-mismatched single-stranded DNA + H2O | SMUG1 is specific for ssDNA substrates, substrate recognition by family-3 SMUG, modelling, detailed overview | Homo sapiens | uracil + single-stranded DNA with abasic site | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | primary and secondary structure, and structural studies of ligand complexes, overview | Escherichia coli |
| More | primary and secondary structure, and structural studies of ligand complexes, overview | Homo sapiens |
| More | primary and secondary structure, and structural studies of ligand complexes, overview | Human alphaherpesvirus 1 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| single-strand-selective mono-functional uracil-DNA glycosylase | - |
Homo sapiens |
| SMUG1 | - |
Homo sapiens |
| UDG | - |
Escherichia coli |
| UDG | - |
Homo sapiens |
| UDG | - |
Human alphaherpesvirus 1 |
| uracil-DNA glycosylase | - |
Escherichia coli |
| uracil-DNA glycosylase | - |
Homo sapiens |
| uracil-DNA glycosylase | - |
Human alphaherpesvirus 1 |
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