Ontology highlight
ABSTRACT:
SUBMITTER: Lahoud G
PROVIDER: S-EPMC3138561 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
Lahoud Georges G Goto-Ito Sakurako S Yoshida Ken-Ichi K Ito Takuhiro T Yokoyama Shigeyuki S Hou Ya-Ming YM
RNA (New York, N.Y.) 20110520 7
Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N(1) of G37, using catalytic motifs that share no sequence or structural homology. Here we show that natural and synthetic analogs of AdoMet are unable to distinguish TrmD from Trm5. Instead, fragments of AdoMet, adenosine and methionine, are selectively inhibitory of TrmD rather than Trm5. Detailed structural information of the two enzy ...[more]