| Literature DB >> 19362833 |
Oscar M Saavedra1, Ljubomir Isakovic, David B Llewellyn, Lijie Zhan, Naomy Bernstein, Stephen Claridge, Franck Raeppel, Arkadii Vaisburg, Nadine Elowe, Andrea J Petschner, Jubrail Rahil, Norman Beaulieu, A Robert MacLeod, Daniel Delorme, Jeffrey M Besterman, Amal Wahhab.
Abstract
The inhibitory activity of base-modified SAH analogues and the specificity of inhibiting human DNMT1 and DNMT3b2 enzymes was explored. The 6-amino group was essential while the 7-N of the adenine ring of SAH could be replaced by CH- without loss of activity against both enzymes. The introduction of small groups at the 2-position of the adenine moiety favors DNMT1 over DNMT3b2 inhibition whereas alkylation of the N(6)-amino moiety favors the inhibition of DNMT3b2 enzyme.Entities:
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Year: 2009 PMID： 19362833 DOI： 10.1016/j.bmcl.2009.03.113
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823