Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning

Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazino...

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Autores principales: Yamamoto, Kohji, Yamaguchi, Misuzu, Yamada, Naotaka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pesticide Science Society of Japan 2020
Materias:
Note
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7691559/
https://www.ncbi.nlm.nih.gov/pubmed/33304193
http://dx.doi.org/10.1584/jpestics.D20-036
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author Yamamoto, Kohji
Yamaguchi, Misuzu
Yamada, Naotaka
author_facet Yamamoto, Kohji
Yamaguchi, Misuzu
Yamada, Naotaka
author_sort Yamamoto, Kohji
collection PubMed
description Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.
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spelling pubmed-76915592020-12-09 Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning Yamamoto, Kohji Yamaguchi, Misuzu Yamada, Naotaka J Pestic Sci Note Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity. Pesticide Science Society of Japan 2020-11-20 /pmc/articles/PMC7691559/ /pubmed/33304193 http://dx.doi.org/10.1584/jpestics.D20-036 Text en © 2020 Pesticide Science Society of Japan https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) License.
spellingShingle Note
Yamamoto, Kohji
Yamaguchi, Misuzu
Yamada, Naotaka
Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title_full Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title_fullStr Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title_full_unstemmed Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title_short Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
title_sort investigation of the active site of an unclassified glutathione transferase in bombyx mori by alanine scanning
topic Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7691559/
https://www.ncbi.nlm.nih.gov/pubmed/33304193
http://dx.doi.org/10.1584/jpestics.D20-036
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