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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q145N6_PARXL Q145N6_PARXL] | | [https://www.uniprot.org/uniprot/Q145N6_PARXL Q145N6_PARXL] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Late-stage methylation is a key technology in the development of pharmaceutical compounds. Methyltransferase biocatalysis may provide powerful options to insert methyl groups into complex molecules with high regio- and chemo-selectivity. The challenge of a large-scale application of methyltransferases is their dependence on S-adenosylmethionine (SAM) as a stoichiometric, and thus exceedingly expensive co-substrate. As a solution to this problem, we and others have explored the use of methyl halides as reagents for in-situ regeneration of SAM. However, the need to handle volatile electrophiles such as methyl iodide (MeI) may also hamper applications at scale. As a more practical solution, we have now developed an enzyme-catalyzed process that affords regeneration of SAM with methyl toluene sulfonate. In this report we describe enzymes from the thiopurine methyltransferase family that accept sulfate- and sulfonate-based methyl donors to convert S-adenosylhomocysteine to SAM with efficiencies that rival MeI-based reactions.
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| Synthetic reagents for enzyme-catalyzed methylation.,Wen X, Leisinger F, Leopold V, Seebeck FP Angew Chem Int Ed Engl. 2022 Aug 21. doi: 10.1002/anie.202208746. PMID:35989225<ref>PMID:35989225</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8ajp" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
