SAM-dependent methyltransferase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='450' side='right' scene='51/510230/Cv/3' caption='SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate [[3ou6]]'> |
== 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>. | ||
Revision as of 05:40, 3 October 2017
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3D structures of SAM-dependent methyltrasferase
Updated on 03-October-2017
References
- ↑ 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
- ↑ Djordjevic S, Stock AM. Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
- ↑ 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
