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- W2100071542 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." @default.
- W2100071542 created "2016-06-24" @default.
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- W2100071542 date "2003-06-01" @default.
- W2100071542 modified "2023-10-13" @default.
- W2100071542 title "Many paths to methyltransfer: a chronicle of convergence" @default.
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- W2100071542 doi "https://doi.org/10.1016/s0968-0004(03)00090-2" @default.
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