Carboxyl Methyltransferase Catalysed Formation of Mono‐ and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis

Abstract: 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 Aspergillus fumigatus 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‐l‐tyrosine, trans, trans‐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).

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Carboxyl Methyltransferase Catalysed Formation of Mono‐ and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis ; day:16 ; month:02 ; year:2022 ; extent:1
Angewandte Chemie / International edition. International edition ; (16.02.2022) (gesamt 1)

Creator
Ward, Lucy C.
McCue, Hannah V.
Rigden, Daniel J.
Kershaw, Neil M.
Ashbrook, Chloe
Hatton, Harry
Goulding, Ellie
Johnson, James R.
Carnell, Andrew J.

DOI
10.1002/anie.202117324
URN
urn:nbn:de:101:1-2022021714044131533797
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:30 AM CEST

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Associated

  • Ward, Lucy C.
  • McCue, Hannah V.
  • Rigden, Daniel J.
  • Kershaw, Neil M.
  • Ashbrook, Chloe
  • Hatton, Harry
  • Goulding, Ellie
  • Johnson, James R.
  • Carnell, Andrew J.

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