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A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms

Small-molecule carboxyl methyltransferases (CbMTs) constitute a small proportion of the reported methyltransferases, but they have received extensive attention due to their important physiological functions. Most of the small-molecule CbMTs isolated to date originate from plants and are members of t...

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Autores principales: Lin, Zhi, Hu, Zhiwei, Zhou, Linjun, Liu, Benben, Huang, Xiaowei, Deng, Zixin, Qu, Xudong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10193983/
https://www.ncbi.nlm.nih.gov/pubmed/37155856
http://dx.doi.org/10.1073/pnas.2301389120
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author Lin, Zhi
Hu, Zhiwei
Zhou, Linjun
Liu, Benben
Huang, Xiaowei
Deng, Zixin
Qu, Xudong
author_facet Lin, Zhi
Hu, Zhiwei
Zhou, Linjun
Liu, Benben
Huang, Xiaowei
Deng, Zixin
Qu, Xudong
author_sort Lin, Zhi
collection PubMed
description Small-molecule carboxyl methyltransferases (CbMTs) constitute a small proportion of the reported methyltransferases, but they have received extensive attention due to their important physiological functions. Most of the small-molecule CbMTs isolated to date originate from plants and are members of the SABATH family. In this study, we identified a type of CbMT (OPCMT) from a group of Mycobacteria, which has a distinct catalytic mechanism from the SABATH methyltransferases. The enzyme contains a large hydrophobic substrate-binding pocket (~400 Å(3)) and utilizes two conserved residues, Thr20 and Try194, to retain the substrate in a favorable orientation for catalytic transmethylation. The OPCMT_like MTs have a broad substrate scope and can accept diverse carboxylic acids enabling efficient production of methyl esters. They are widely (more than 10,000) distributed in microorganisms, including several well-known pathogens, whereas no related genes are found in humans. In vivo experiments implied that the OPCMT_like MTs was indispensable for M. neoaurum, suggesting that these proteins have important physiological functions.
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spelling pubmed-101939832023-11-08 A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms Lin, Zhi Hu, Zhiwei Zhou, Linjun Liu, Benben Huang, Xiaowei Deng, Zixin Qu, Xudong Proc Natl Acad Sci U S A Biological Sciences Small-molecule carboxyl methyltransferases (CbMTs) constitute a small proportion of the reported methyltransferases, but they have received extensive attention due to their important physiological functions. Most of the small-molecule CbMTs isolated to date originate from plants and are members of the SABATH family. In this study, we identified a type of CbMT (OPCMT) from a group of Mycobacteria, which has a distinct catalytic mechanism from the SABATH methyltransferases. The enzyme contains a large hydrophobic substrate-binding pocket (~400 Å(3)) and utilizes two conserved residues, Thr20 and Try194, to retain the substrate in a favorable orientation for catalytic transmethylation. The OPCMT_like MTs have a broad substrate scope and can accept diverse carboxylic acids enabling efficient production of methyl esters. They are widely (more than 10,000) distributed in microorganisms, including several well-known pathogens, whereas no related genes are found in humans. In vivo experiments implied that the OPCMT_like MTs was indispensable for M. neoaurum, suggesting that these proteins have important physiological functions. National Academy of Sciences 2023-05-08 2023-05-16 /pmc/articles/PMC10193983/ /pubmed/37155856 http://dx.doi.org/10.1073/pnas.2301389120 Text en Copyright © 2023 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Biological Sciences
Lin, Zhi
Hu, Zhiwei
Zhou, Linjun
Liu, Benben
Huang, Xiaowei
Deng, Zixin
Qu, Xudong
A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title_full A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title_fullStr A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title_full_unstemmed A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title_short A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
title_sort large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
topic Biological Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10193983/
https://www.ncbi.nlm.nih.gov/pubmed/37155856
http://dx.doi.org/10.1073/pnas.2301389120
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