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Issue 81, 2017
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A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

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We herein report the first covalent G-site-binding inhibitor for GST, GS-ESF (1), which irreversibly inhibited the GSTP1-1 function. LC-MS/MS and X-ray structure analyses of the covalently linked GST-inhibitor complex suggested that 1 reacted with Tyr108 of GSTP1-1. The mechanism of covalent bond formation was discussed based on MD simulation results.

Graphical abstract: A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

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Publication details

The article was received on 26 Jul 2017, accepted on 19 Aug 2017 and first published on 21 Aug 2017

Article type: Communication
DOI: 10.1039/C7CC05829B
Citation: Chem. Commun., 2017,53, 11138-11141
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    A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1)

    Y. Shishido, F. Tomoike, Y. Kimura, K. Kuwata, T. Yano, K. Fukui, H. Fujikawa, Y. Sekido, Y. Murakami-Tonami, T. Kameda, S. Shuto and H. Abe, Chem. Commun., 2017, 53, 11138
    DOI: 10.1039/C7CC05829B

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