A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms
Autor: | Zhi Lin, Zhiwei Hu, Linjun Zhou, Benben Liu, Xiaowei Huang, Zixin Deng, Xudong Qu |
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Rok vydání: | 2023 |
Předmět: | |
Zdroj: | Proceedings of the National Academy of Sciences. 120 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.2301389120 |
Popis: | 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. |
Databáze: | OpenAIRE |
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