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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.

SUBMITTER: Schubert HL

PROVIDER: S-EPMC2758044 | biostudies-literature | 2003 Jun

REPOSITORIES: biostudies-literature

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Many paths to methyltransfer: a chronicle of convergence.

Schubert Heidi L HL Blumenthal Robert M RM Cheng Xiaodong X

Trends in biochemical sciences 20030601 6

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 ...[more]

PMID: 12826405

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