From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases |
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Authors: | Dr Qingyun Tang Assist?Prof?Dr Ioannis V Pavlidis Dr Christoffel P S Badenhorst Prof?Dr Uwe T Bornscheuer |
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Affiliation: | 1. Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17489 Greifswald, Germany;2. Dept. of Chemistry, University of Crete, Voutes University Campus, 70013 Heraklion, Greece |
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Abstract: | Halide methyltransferases (HMTs) enable the enzymatic synthesis of S-adenosyl-l -methionine (SAM) from S-adenosyl-l -homocysteine (SAH) and methyl iodide. Characterisation of a range of naturally occurring HMTs and subsequent protein engineering led to HMT variants capable of synthesising ethyl, propyl, and allyl analogues of SAM. Notably, HMTs do not depend on chemical synthesis of methionine analogues, as required by methionine adenosyltransferases (MATs). However, at the moment MATs have a much broader substrate scope than the HMTs. Herein we provide an overview of the discovery and engineering of promiscuous HMTs and how these strategies will pave the way towards a toolbox of HMT variants for versatile chemo- and regioselective biocatalytic alkylations. |
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Keywords: | alkylation alkyl iodide halide methyltransferase methylation SAM analogue |
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