Many Paths to Methyltransfer: a Chronicle of Convergence

Overview

Journal Trends Biochem Sci

Specialty Biochemistry

Date 2003 Jun 27

PMID 12826405

Citations 434

Authors

Heidi L Schubert

Robert M Blumenthal

Xiaodong Cheng

Affiliations

Soon will be listed here.

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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