Ontology highlight
ABSTRACT:
SUBMITTER: Wang R
PROVIDER: S-EPMC3104021 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Wang Rui R Zheng Weihong W Yu Haiqiang H Deng Haiteng H Luo Minkui M
Journal of the American Chemical Society 20110503 20
Elucidating physiological and pathogenic functions of protein methyltransferases (PMTs) relies on knowing their substrate profiles. S-adenosyl-L-methionine (SAM) is the sole methyl-donor cofactor of PMTs. Recently, SAM analogues have emerged as novel small-molecule tools to efficiently label PMT substrates. Here we reported the development of a clickable SAM analogue cofactor, 4-propargyloxy-but-2-enyl SAM, and its implementation to label substrates of human protein arginine methyltransferase 1 ...[more]