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Literature summary for 2.1.1.113 extracted from
- Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment (1997), Nucleic Acids Res., 25, 2702-2715.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| determination of the structure of PvuII methyltransferase complexed with S-adenosyl-L-methionine by multiwavelength anomalous diffraction using a crystal of the selenomethionine substituted protein | Proteus vulgaris |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Proteus vulgaris | - |
enzyme M.PvuII | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + [DNA]-cytosine | the enzyme catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the exocyclic aminoN4 nitrogen of the central cytosine in its recognition sequence 5'-CAGCTG-3' | Proteus vulgaris | S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| M.PvuII | - |
Proteus vulgaris |
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Release 2023.1 (January 2023)
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