Many paths to methyltransfer: a chronicle of convergence
- PMID: 12826405
- PMCID: PMC2758044
- DOI: 10.1016/S0968-0004(03)00090-2
Many paths to methyltransfer: a chronicle of convergence
Abstract
S-adenosyl-L-methionine (AdoMet) dependent methyltransferases (MTases) are involved in biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing. Five different structural folds (I-V) have been described that bind AdoMet and catalyze methyltransfer to diverse substrates, although the great majority of known MTases have the Class I fold. Even within a particular MTase class the amino-acid sequence similarity can be as low as 10%. Thus, the structural and catalytic requirements for methyltransfer from AdoMet appear to be remarkably flexible.
Figures
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