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Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase

The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione wi...

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Detalles Bibliográficos
Autores principales: Hossain, M. D. Tofazzal, Yamada, Naotaka, Yamamoto, Kohji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029803/
https://www.ncbi.nlm.nih.gov/pubmed/24848539
http://dx.doi.org/10.1371/journal.pone.0097740
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author Hossain, M. D. Tofazzal
Yamada, Naotaka
Yamamoto, Kohji
author_facet Hossain, M. D. Tofazzal
Yamada, Naotaka
Yamamoto, Kohji
author_sort Hossain, M. D. Tofazzal
collection PubMed
description The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and 4-nitrophenethyl bromide. Mutagenesis of highly conserved residues in the catalytic site revealed that Glu66 and Ser67 are important for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTT and into the metabolism of exogenous chemical agents.
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spelling pubmed-40298032014-05-28 Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase Hossain, M. D. Tofazzal Yamada, Naotaka Yamamoto, Kohji PLoS One Research Article The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and 4-nitrophenethyl bromide. Mutagenesis of highly conserved residues in the catalytic site revealed that Glu66 and Ser67 are important for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTT and into the metabolism of exogenous chemical agents. Public Library of Science 2014-05-21 /pmc/articles/PMC4029803/ /pubmed/24848539 http://dx.doi.org/10.1371/journal.pone.0097740 Text en © 2014 Hossain et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Hossain, M. D. Tofazzal
Yamada, Naotaka
Yamamoto, Kohji
Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title_full Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title_fullStr Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title_full_unstemmed Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title_short Glutathione-Binding Site of a Bombyx mori Theta-Class Glutathione Transferase
title_sort glutathione-binding site of a bombyx mori theta-class glutathione transferase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4029803/
https://www.ncbi.nlm.nih.gov/pubmed/24848539
http://dx.doi.org/10.1371/journal.pone.0097740
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