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SAM-dependent methyltransferase

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== Function ==
== 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)<ref>PMID:23180741</ref>.
'''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)<ref>PMID:23180741</ref>.
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For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playgroun]d/CheR]].<ref>PMID:9628482</ref>.<br />
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For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>.<br />
*SEE ALSO [[Chemotaxis protein]].
*SEE ALSO [[Chemotaxis protein]].

Revision as of 08:16, 23 August 2016

SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate 3ou6

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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
  2. ↑ Djordjevic S, Stock AM. Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
  3. ↑ Lee JH, Bae B, Kuemin M, Circello BT, Metcalf WW, Nair SK, van der Donk WA. Characterization and structure of DhpI, a phosphonate O-methyltransferase involved in dehydrophos biosynthesis. Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17557-62. Epub 2010 Sep 27. PMID:20876132 doi:10.1073/pnas.1006848107

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