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. 2018 Aug 28;17:131. doi: 10.1186/s12934-018-0978-8

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© The Author(s) 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — In vitro characterization of TubG as a Nudix hydrolase responsible for the final hydrolysis step. a Schematic of the TubG-catalyzed reaction using the analog of 5, AMP, as substrate. b HPLC traces of the TubG reaction. Std, the authentic standards of AMP and adenosine; TubG, HPLC traces of the TubG reaction with AMP as substrate; N.C, EIC analysis of the reaction with AMP as substrate added but without TubG added. c Relative activity of TubG with AMP as substrate and different divalent cations as metallic cofactor