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Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins

Cite this: Biochemistry 2018, 57, 25, 3515–3523
Publication Date (Web):April 25, 2018
https://doi.org/10.1021/acs.biochem.8b00296
Copyright © 2018 American Chemical Society
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Abstract

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Methanobactins (Mbns) are ribosomally produced, post-translationally modified bacterial natural products with a high affinity for copper. MbnN, a pyridoxal 5′-phosphate-dependent aminotransferase, performs a transamination reaction that is the last step in the biosynthesis of Mbns produced by several Methylosinus species. Our bioinformatic analyses indicate that MbnNs likely derive from histidinol-phosphate aminotransferases (HisCs), which play a key role in histidine biosynthesis. A comparison of the HisC active site with the predicted MbnN structure suggests that MbnN’s active site is altered to accommodate the larger and more hydrophobic substrates necessary for Mbn biosynthesis. Moreover, we have confirmed that MbnN is capable of catalyzing the final transamination step in Mbn biosynthesis in vitro and in vivo. We also demonstrate that without this final modification, Mbn exhibits significantly decreased stability under physiological conditions. An examination of other Mbns and Mbn operons suggests that N-terminal protection of this family of natural products is of critical importance and that several different means of N-terminal stabilization have evolved independently in Mbn subfamilies.

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The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.biochem.8b00296.

  • Extended materials and methods, Figures S1–S13, and Tables S1–S4 (PDF)

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Cited By

This article is cited by 5 publications.

  1. Luis F. Schachner, Ashley N. Ives, John P. McGee, Rafael D. Melani, Jared O. Kafader, Philip D. Compton, Steven M. Patrie, Neil L. Kelleher. Standard Proteoforms and Their Complexes for Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2019, 30 (7) , 1190-1198. https://doi.org/10.1021/jasms.8b06040
  2. Nilkamal Mahanta, D. Miklos Szantai-Kis, E. James Petersson, Douglas A. Mitchell. Biosynthesis and Chemical Applications of Thioamides. ACS Chemical Biology 2019, 14 (2) , 142-163. https://doi.org/10.1021/acschembio.8b01022
  3. Jeremy D Semrau, Alan A DiSpirito, Parthiba Karthikeyan Obulisamy, Christina S Kang-Yun. Methanobactin from methanotrophs: genetics, structure, function and potential applications. FEMS Microbiology Letters 2020, 367 (5) https://doi.org/10.1093/femsle/fnaa045
  4. Grace E. Kenney, Laura M. K. Dassama, Anastasia C. Manesis, Matthew O. Ross, Siyu Chen, Brian M. Hoffman, Amy C. Rosenzweig. MbnH is a diheme MauG-like protein associated with microbial copper homeostasis. Journal of Biological Chemistry 2019, 294 (44) , 16141-16151. https://doi.org/10.1074/jbc.RA119.010202
  5. Yi-Ling Du, Katherine S. Ryan. Pyridoxal phosphate-dependent reactions in the biosynthesis of natural products. Natural Product Reports 2019, 36 (3) , 430-457. https://doi.org/10.1039/C8NP00049B

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