Enzymatic S‐methylation of thiols catalyzed by different O‐methyltransferases

Abstract: S-Adenosyl-l-methionine (SAM)-dependent methyltransferases (MTs) are highly chemoselective enzymes grouped in C-, N-, O-, S- and halide MTs, depending on the (hetero) atom that acts as the methyl group acceptor. So far, OMTs present the largest group, including many well investigated candidates. The catechol OMT from mammals such as from Rattus norvegicus (RnCOMT) is involved in the metabolism of neurotransmitters like dopamine. It is known to methylate the hydroxyl of the catechol ring in the 3 position. There are also reports showing that the regioselectivity of different COMTs can vary leading to different products with methyl groups in the 3 and or 4 positions. Nevertheless, there was only O-methylation reported for COMTs. Another related MT, the caffeate OMT involved in the lignin biosynthesis of plants has also been reported as a chemoselective enzyme. In nature, S-methylation is a rare phenomenon with different methyl donors being involved in the methyl transfer onto sulfur atoms. Several SAM-dependent MTs are identified as S-methyltransferases (SMTs), these are involved in salvaging pathways and xenobiotic metabolism of cells. Here, we report a new function of three OMTs; RnCOMT, a COMT from Myxococcus xanthus (MxSafC), and a CaOMT from Prunus persica (PpCaOMT) with acceptance towards different aromatic thiol substrates with up to full conversion

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch
Notes
ChemCatChem. - 16, 2 (2024) , e202301217, ISSN: 1867-3899

Event
Veröffentlichung
(where)
Freiburg
(who)
Universität
(when)
2024
Creator

DOI
10.1002/cctc.202301217
URN
urn:nbn:de:bsz:25-freidok-2545521
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
25.03.2025, 1:45 PM CET

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Time of origin

  • 2024

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