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Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases

Methyltransferases (MTases) play an important role in the functioning of living systems, catalyzing the methylation reactions of DNA, RNA, proteins, and small molecules, including endogenous compounds and drugs. Many human diseases are associated with disturbances in the functioning of these enzymes...

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Detalles Bibliográficos
Autores principales: Rudenko, A. Yu., Mariasina, S. S., Sergiev, P. V., Polshakov, V. I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pleiades Publishing 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9009987/
https://www.ncbi.nlm.nih.gov/pubmed/35440827
http://dx.doi.org/10.1134/S002689332202011X
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author Rudenko, A. Yu.
Mariasina, S. S.
Sergiev, P. V.
Polshakov, V. I.
author_facet Rudenko, A. Yu.
Mariasina, S. S.
Sergiev, P. V.
Polshakov, V. I.
author_sort Rudenko, A. Yu.
collection PubMed
description Methyltransferases (MTases) play an important role in the functioning of living systems, catalyzing the methylation reactions of DNA, RNA, proteins, and small molecules, including endogenous compounds and drugs. Many human diseases are associated with disturbances in the functioning of these enzymes; therefore, the study of MTases is an urgent and important task. Most MTases use the cofactor S‑adenosyl‑L‑methionine (SAM) as a methyl group donor. SAM analogs are widely applicable in the study of MTases: they are used in studies of the catalytic activity of these enzymes, in identification of substrates of new MTases, and for modification of the substrates or substrate linking to MTases. In this review, new synthetic analogs of SAM and the problems that can be solved with their usage are discussed.
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spelling pubmed-90099872022-04-15 Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases Rudenko, A. Yu. Mariasina, S. S. Sergiev, P. V. Polshakov, V. I. Mol Biol Reviews Methyltransferases (MTases) play an important role in the functioning of living systems, catalyzing the methylation reactions of DNA, RNA, proteins, and small molecules, including endogenous compounds and drugs. Many human diseases are associated with disturbances in the functioning of these enzymes; therefore, the study of MTases is an urgent and important task. Most MTases use the cofactor S‑adenosyl‑L‑methionine (SAM) as a methyl group donor. SAM analogs are widely applicable in the study of MTases: they are used in studies of the catalytic activity of these enzymes, in identification of substrates of new MTases, and for modification of the substrates or substrate linking to MTases. In this review, new synthetic analogs of SAM and the problems that can be solved with their usage are discussed. Pleiades Publishing 2022-04-14 2022 /pmc/articles/PMC9009987/ /pubmed/35440827 http://dx.doi.org/10.1134/S002689332202011X Text en © Pleiades Publishing, Inc. 2022, ISSN 0026-8933, Molecular Biology, 2022, Vol. 56, No. 2, pp. 229–250. © Pleiades Publishing, Inc., 2022.Russian Text © The Author(s), 2022, published in Molekulyarnaya Biologiya, 2022, Vol. 56, No. 2, pp. 296–319. This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Reviews
Rudenko, A. Yu.
Mariasina, S. S.
Sergiev, P. V.
Polshakov, V. I.
Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title_full Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title_fullStr Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title_full_unstemmed Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title_short Analogs of S-Adenosyl-L-Methionine in Studies of Methyltransferases
title_sort analogs of s-adenosyl-l-methionine in studies of methyltransferases
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9009987/
https://www.ncbi.nlm.nih.gov/pubmed/35440827
http://dx.doi.org/10.1134/S002689332202011X
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