SAM-dependent methyltransferase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='51/510230/Cv/3' caption='SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate [[3ou6]]'> | |||
== 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). | '''SAM-dependent methyltransferase''' or '''S-adenosylmethionine-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''')<ref>PMID:23180741</ref>. | ||
For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>.<br /> | |||
*SEE ALSO [[Chemotaxis protein]]. | |||
== Structural highlights == | |||
The <scene name='51/510230/Cv/5'>core of the SDM fold contains alternating β strands and α helices</scene>. SDM <scene name='51/510230/Cv/6'>active site is located between the 2 monomers</scene><ref>PMID:20876132</ref>. Water molecules are shown as red spheres. | |||
==3D structures of SAM-dependent methyltrasferase== | ==3D structures of SAM-dependent methyltrasferase== | ||
[[SAM-dependent methyltrasferase 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | |||
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Latest revision as of 09:25, 11 August 2024
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