SAM-dependent methyltransferase
From Proteopedia
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3D structures of SAM-dependent methyltrasferase
Updated on 21-January-2020
FunctionSAM-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].
For Chemotaxis receptor methyltransferase CheR see details in Molecular Playground/CheR.[2].
Structural highlightsThe core of the SDM fold contains alternating β strands and α helices. SDM active site is located between the 2 monomers[3]. Water molecules are shown as red spheres. 3D structures of SAM-dependent methyltrasferaseSAM-dependent methyltrasferase 3D structures
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Updated on 21-January-2020
This page was last modified 08:59, 21 January 2020.