SAM-dependent methyltransferase
From Proteopedia
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{{STRUCTURE_3h2b| PDB=3h2b | SIZE=400| SCENE= |right|CAPTION=SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and pyrophosphate, [[3h2b]] }} | {{STRUCTURE_3h2b| PDB=3h2b | SIZE=400| SCENE= |right|CAPTION=SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and pyrophosphate, [[3h2b]] }} | ||
| - | + | == 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). The core of the SDM fold contains alternating β strands and α helices | + | '''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>. See also [[Molecular Playground/CheR]]. |
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| + | == Structural highlights == | ||
| + | The core of the SDM fold contains alternating β strands and α helices. | ||
==3D structures of SAM-dependent methyltrasferase== | ==3D structures of SAM-dependent methyltrasferase== | ||
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**[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br /> | **[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br /> | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:45, 23 August 2016
Contents |
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)[1]. See also Molecular Playground/CheR.
Structural highlights
The core of the SDM fold contains alternating β strands and α helices.
3D structures of SAM-dependent methyltrasferase
Updated on 23-August-2016
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
