title: 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.
authors.affiliation: Department of Biochemistry, University of Utah, Salt Lake City 84132-3201, USA. heidi@biochem.utah.edu
authors.forename: Heidi L
authors.initials: HL
authors.lastname: Schubert
authors.forename: Robert M
authors.initials: RM
authors.lastname: Blumenthal
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000235:genetics; D019175:DNA Methylation; D006801:Humans; D008780:Methyltransferases / Q000737:chemistry* / Q000502:physiology*; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012436:S-Adenosylmethionine / Q000378:metabolism
chemical_list: D012436:S-Adenosylmethionine; D008780:Methyltransferases