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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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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. |
format | Online Article Text |
id | pubmed-4029803 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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