Ontology highlight
ABSTRACT:
SUBMITTER: Sakaguchi R
PROVIDER: S-EPMC4224600 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Sakaguchi Reiko R Lahoud Georges G Christian Thomas T Gamper Howard H Hou Ya-Ming YM
Chemistry & biology 20140911 10
The catalytic mechanism of the majority of S-adenosyl methionine (AdoMet)-dependent methyl transferases requires no divalent metal ions. Here we report that methyl transfer from AdoMet to N(1) of G37-tRNA, catalyzed by the bacterial TrmD enzyme, is strongly dependent on divalent metal ions and that Mg(2+) is the most physiologically relevant. Kinetic isotope analysis, metal rescue, and spectroscopic measurements indicate that Mg(2+) is not involved in substrate binding, but in promoting methyl t ...[more]