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Trends Biochem Sci. 2003 Jun;28(6):329-35.

Many paths to methyltransfer: a chronicle of convergence.

Author information

1
Department of Biochemistry, University of Utah, Salt Lake City 84132-3201, USA. heidi@biochem.utah.edu

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.

PMID:
12826405
PMCID:
PMC2758044
DOI:
10.1016/S0968-0004(03)00090-2
[Indexed for MEDLINE]
Free PMC Article

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