Functional characterization of a naphthalene-O-methyltransferase from Nocardia sp. CS682

Methylation plays important roles in biosynthesis, metabolism, signal transduction, detoxification, protein sorting and repair, and nucleic acid processing. Generally the methyltransferases transfer methyl groups in various natural products using S-adenosyl methionine (SAM) as a cofactor. In this study, we examined and functionally characterized ThnM3 (enzyme), by testing various substrates with different chemical structures. Among the tested substrates, 1,8-dihydroxynaphthalene was the best substrate for methylation. Whole-cell biotransformation was performed using the enzyme in engineered Escherichia coli to produce 8-methoxynaphthalene-1-ol, and 1,8-dimethoxynaphthalene derivatives of 1,8-dihydroxynaphthalene. The products were confirmed using high-performance liquid chromatography, mass spectrometry, and nuclear magnetic resonance spectroscopic analyses. Therefore, this study is the first to amplify, express the thnM3 (gene), and functionally characterize theThnM3, which exhibits the regioselective modifications of 1,8-dihydroxynaphthalene.