SAM-dependent methyltransferase

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Template:STRUCTURE 3h2b

SAM-dependent methyltransferase (SDM) utilizes the methyl donor S-adenosyl-L-methionine (SAM) as a cofactor to methylate proteins, small molecules, lipids and nucleic acids. SAM forms S-adenosyl-L-homocysteine (SAH) upon demethylation. About 120 members of the SDM family have been identified. They differ in their substrate specificity and the atom targeted for methylation (N, O, C, S). The core of the SDM fold contains alternating β strands and α helices. See also Molecular Playground/CheR.

3D structures of SAM-dependent methyltrasferase

Updated on 10-December-2014

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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