SAM-dependent methyltransferase
From Proteopedia
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.
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3D structures of SAM-dependent methyltrasferase
SAM-dependent O-methyltransferase
1o54 – TmSDM – Thermotoga maritima
2hnk – SDM – Leptospira interrogans
3r3h – SDM – Legionella pneumophila
SAM-dependent N-methyltransferase
1vlm – TmSDM (mutant)
SAM-dependent methyltransferase
1wzn – SDM – Pyrococcus horikoshii
2igt – SDM – Agrobacterium tumefaciens
3cgg – CgSDM – Corynebacterium glutamicum
3d2l - SDM – Exiguobacterium sibiricum
3dh0 - SDM – Aquifex aeolicus
3dp7 - SDM – Bacterioides vulgatus
3ggd - SDM – Anabaena variabilis
3sm3 - SDM (mutant) – Methanosarcina mazei
3h2b – CgSDM + pyrophosphate + SAH