S-Adenosyl methionine (SAM or AdoMet) consists of an adenosyl cation attached to the sulfur methionine.
It is synthesized from ATP and methionine by S-Adenosylmethionine synthetase enzyme through the
the reaction of ATP with L-methionine and water forming as catalytical product S-adenosyl-L-methionine.
SAM is a common cosubstrate involved in several reactions, among which methyl group transfers.
Trm1 di-methylates a single guanine residue at position 26 of most tRNAs using SAM as a donor
of the methyl groups, and is required for the modification of both mitochondrial and cytoplasmic tRNAs.
Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae.
Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae.