Ward, Lucy C, McCue, Hannah V, Rigden, Daniel J 
ORCID: 0000-0002-7565-8937, Kershaw, Neil M, Ashbrook, Chloe, Hatton, Harry, Goulding, Ellie, Johnson, James R and Carnell, Andrew J ORCID: 0000-0002-6353-403X
(2022)
Carboxyl Methyltransferase Catalysed Formation of Mono‐ and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis.
Angewandte Chemie, 134 (14).
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Abstract
<jats:title>Abstract</jats:title><jats:p>Carboxyl methyltransferase (CMT) enzymes catalyse the biomethylation of carboxylic acids under aqueous conditions and have potential for use in synthetic enzyme cascades. Herein we report that the enzyme FtpM from <jats:italic>Aspergillus fumigatus</jats:italic> can methylate a broad range of aromatic mono‐ and dicarboxylic acids in good to excellent conversions. The enzyme shows high regioselectivity on its natural substrate fumaryl‐<jats:sc>l</jats:sc>‐tyrosine, <jats:italic>trans</jats:italic>, <jats:italic>trans</jats:italic>‐muconic acid and a number of the dicarboxylic acids tested. Dicarboxylic acids are generally better substrates than monocarboxylic acids, although some substituents are able to compensate for the absence of a second acid group. For dicarboxylic acids, the second methylation shows strong pH dependency with an optimum at pH 5.5–6. Potential for application in industrial biotechnology was demonstrated in a cascade for the production of a bioplastics precursor (FDME) from bioderived 5‐hydroxymethylfurfural (HMF).</jats:p>
| Item Type: | Article |
|---|---|
| Divisions: | Faculty of Science and Engineering > School of Physical Sciences |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 11 Feb 2022 08:52 |
| Last Modified: | 25 Aug 2023 07:56 |
| DOI: | 10.1002/ange.202117324 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3148744 |
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