Histidine methylation <i>via</i> an enzymatic cascade with <i>in situ</i> generation of nucleoside-modified AdoMet analogues

Histidine methyltransferases (HMTs) are AdoMet-dependent enzymes that catalyse regioselective methylation of histidine residues in proteins. Here, we demonstrate that a methionine adenosyltransferase (MAT)/HMT cascade system enables the generation and utilisation of AdoMet analogues for efficient and selective histidine methylation in peptide substrates.

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Publication Details

Journal
Chemical Communications
Published
2025-12-30
DOI
https://doi.org/10.1039/d5cc06375b
Primary Topic
Cancer-related gene regulation
Type
article
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article

Histidine methylation via an enzymatic cascade with in situ generation of nucleoside-modified AdoMet analogues

Jasmin Mecinović, Andrea Rentmeister, Jakub Drożak, Marija Ram et al.
Chemical Communications
Cancer-related gene regulation
article

Histidine methylation via an enzymatic cascade with in situ generation of nucleoside-modified AdoMet analogues

Jasmin Mecinović, Andrea Rentmeister, Jakub Drożak, Marija Ram, Arne Hoffmann, Antonia L. Irion, Zhimei Yu
article en

Abstract

Histidine methyltransferases (HMTs) are AdoMet-dependent enzymes that catalyse regioselective methylation of histidine residues in proteins. Here, we demonstrate that a methionine adenosyltransferase (MAT)/HMT cascade system enables the generation and utilisation of AdoMet analogues for efficient and selective histidine methylation in peptide substrates.

Chemical CommunicationsVol. 62(10)
University of Southern Denmark (DK), University of Warsaw (PL), Ludwig-Maximilians-Universität München (DE)
Openalex Percentile: Top 35%
Cancer-related gene regulation
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Histidine methylation <i>via</i> an enzymatic cascade with <i>in situ</i> generation of nucleoside-modified AdoMet analogues — Jasmin Mecinović, Andrea Rentmeister, et al. · Chemical Communications (2025) | TGRS Research Map | TGRS