 | REBASE References 07/7/2024
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| REBASE Ref Num 9368 entered Apr 10 2006 ... modified Apr 10 2006 |
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Schubert, H.L., Blumenthal, R.M., Cheng, X.; Trends Biochem. Sci. 28: 329-335 (2003). 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. |
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