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From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases
- 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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| Author: | Qingyun Tang, Ioannis V. Pavlidis, Christoffel P. S. Badenhorst, Uwe T. BornscheuerORCiD |
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| URN: | urn:nbn:de:gbv:9-opus-60578 |
| DOI: | https://doi.org/10.1002/cbic.202100153 |
| ISSN: | 1439-7633 |
| Parent Title (English): | ChemBioChem |
| Publisher: | Wiley |
| Place of publication: | Hoboken, NJ |
| Document Type: | Article |
| Language: | English |
| Date of first Publication: | 2021/08/17 |
| Release Date: | 2022/11/30 |
| Tag: | SAM analogue; alkyl iodide; alkylation; halide methyltransferase; methylation |
| Volume: | 22 |
| Issue: | 16 |
| Page Number: | 7 |
| First Page: | 2584 |
| Last Page: | 2590 |
| Faculties: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie |
| Licence (German): |  Creative Commons - Namensnennung |