SAM-dependent methyltransferase

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Contents 1 Function 2 Structural highlights 3 3D structures of SAM-dependent methyltrasferase 4 References

Function

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)^[1]. See also Molecular Playground/CheR.

Structural highlights

The core of the SDM fold contains alternating β strands and α helices.

3D structures of SAM-dependent methyltrasferase

Updated on 23-August-2016

References

1. ↑ Struck AW, Thompson ML, Wong LS, Micklefield J. S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications. Chembiochem. 2012 Dec 21;13(18):2642-55. doi: 10.1002/cbic.201200556. Epub 2012, Nov 23. PMID:23180741 doi:http://dx.doi.org/10.1002/cbic.201200556