Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 19, Pages 5182-5200Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201608625
Keywords
S-adenosyl methionine; DNA functionalization; methyltransferases; protein modification; transalkylation
Categories
Funding
- European Research Council under the European Union [291593 FLUOROCODE, 686271 Ad gut]
- 'Methusalem grant [1404]
- Fonds voor Wetenschapplijk Onderzoek Vlaanderen (FWO) [G0484.12, G0683.15, GOH6316N]
- Industrieel Onderzoeksfonds (IOF) [C32/16/005]
- FWO Flanders [12C2814N, 12C2817N]
- European Union [634890]
- Engineering and Physical Sciences Research Council (EPSRC) [EP/N020901/1]
- Engineering and Physical Sciences Research Council [EP/N020901/1] Funding Source: researchfish
- EPSRC [EP/N020901/1] Funding Source: UKRI
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Methyltransferases (MTases) form a large family of enzymes that methylate a diverse set of targets, ranging from the three major biopolymers to small molecules. Most of these MTases use the cofactor S-adenosyl-l-Methionine (AdoMet) as a methyl source. In recent years, there have been significant efforts toward the development of AdoMet analogues with the aim of transferring moieties other than simple methyl groups. Two major classes of AdoMet analogues currently exist: doubly-activated molecules and aziridine based molecules, each of which employs a different approach to achieve transalkylation rather than transmethylation. In this review, we discuss the various strategies for labelling and functionalizing biomolecules using AdoMet-dependent MTases and AdoMet analogues. We cover the synthetic routes to AdoMet analogues, their stability in biological environments and their application in transalkylation reactions. Finally, some perspectives are presented for the potential use of AdoMet analogues in biology research, (epi)genetics and nanotechnology.
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