EC Number   |
Activating Compound |
Reference |
|---|
    2.1.1.37 | 5-methyl cytosine |
preference for single stranded DNA substrates is increased up to 50fold by the presence of a proximal 5-methyl cytosine. This modulation is distance-dependent and is due to an enhanced binding affinity and minor changes in catalytic efficiency. No modulation of activity is observed with double stranded DNA |
657752 |
| 2.1.1.37 | dimethyl sulfoxide |
stimulates |
658258 |
| 2.1.1.37 | DNA(cytosine-S)-methyltransferase 3-like protein |
i.e. Dnmt3L, UniProt Acc Q09CWR8. Dnmt3L stimulates activity of Dnmt3B by directly binding to the catalytic domain via its own C-terminal domain. The catalytic activity is stimulated about 15fold. Dnmt3L directly binds to DNA but not to S-adenosyl-L-methionine. Dnmt3L acts as a substrate exchange factor that accelerates DNA and AdoMet binding |
659456 |
| 2.1.1.37 | DNA(cytosine-S)-methyltransferase 3-like protein |
i.e. Dnmt3L, UniProt Acc Q09CWR8. Dnmt3L stimulates activity of the Dnmt3A by directly binding to the catalytic domain via its own C-terminal domain. The catalytic activity is stimulated about 15fold. Dnmt3L directly binds to DNA but not to S-adenosyl-L-methionine. Complex formation between Dnmt3A and Dnmt3L accelerates DNA binding by Dnmt3A 20fold and lowers its Km for DNA. Interaction of Dnmt3L with Dnmt3A increases the binding of AdoMet to Dnmt3A, and lowers the Km-value of Dnmt3A for AdoMet. Interaction of Dnmt3A and Dnmt3L is transient, and after DNA binding to Dnmt3A, Dnmt3L dissociates from the complex. Following dissociation of Dnmt3L, Dnmt3A adopts a closed conformation leading to slow rates of DNA release. Therefore, Dnmt3L acts as a substrate exchange factor that accelerates DNA and AdoMet binding |
659456 |
| 2.1.1.37 | methylated DNA |
stimulated methylation spreading on unmethylated CpG sequences for full-length and the mutant lacking 121 N-terminal amino acids equally well. No stimulation of N-terminal deletion mutants lacking 501, 540, or 580 amino acids from the N-terminus |
657995 |
| 2.1.1.37 | more |
no modulation of catalytic activity in response to 5-methyl cytosine |
657752 |
| 2.1.1.37 | NSC 319745 |
activation of Dnmt3b |
702694 |
| 2.1.1.37 | NSC 345763 |
slight activation of Dnmt1 |
702694 |
| 2.1.1.37 | RNAse A |
RNase A treatment increases DNMT1 activity in vitro. The methyltransferase activity on hemimethylated DNA is about 8fold higher compared to control, and 2fold higher on a poly(dI-dC) substrate |
757832 |
| 2.1.1.37 | stimulating proteins |
the proteins from murine P815 mastocytoma cells stimulate both de novo and maintenance activity of DNA methyltransferase about 3fold. They enhance the methylation of any natural DNA and of poly[(dI-dC)*(dI-dC)] but inhibit methylation of poly[(dG-dC)*(dG-dC)] |
485281 |
