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Literature summary for 2.1.1.63 extracted from
- An O6-methylguanine-DNA methyltransferase-like protein from Thermus thermophilus interacts with a nucleotide excision repair protein (2008), J. Biochem., 144, 267-277.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Rosetta(DE3) cells | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
| Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| amylose resin column chromatography, Toyopearl-SuperQ column chromatography, ammonium sulfate precipitation, and Toyopearl-ether 650M column chromatography | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | TTHA1564 can bind to DNA containing 6-O-methylguanine with higher affinity (9fold) than normal (unmethylated) DNA, but TTHA1564 alone does not possess methyltransferase activity | Thermus thermophilus | ? | - |
? |  |
| additional information | TTHA1564 can interact with nucleotide excision repair proteins and RNA polymerase | Thermus thermophilus | ? | - |
? | |
| additional information | TTHA1564 can bind to DNA containing 6-O-methylguanine with higher affinity (9fold) than normal (unmethylated) DNA, but TTHA1564 alone does not possess methyltransferase activity | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
| additional information | TTHA1564 can interact with nucleotide excision repair proteins and RNA polymerase | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| O6-methylguanine-DNA methyltransferase | - |
Thermus thermophilus |
| OGT | - |
Thermus thermophilus |
| TTHA1564 | - |
Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme requires no cofactor | Thermus thermophilus |
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Release 2023.1 (January 2023)
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