Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp
ABSTRACT Glutathione reductase is an important oxidoreductase that helps maintain redox homeostasis by catalyzing the conversion of glutathione disulfide to glutathione using NADPH as a cofactor. In this study, we cloned and characterized a glutathione reductase (hereafter referred to as SpGR) from...
Published in: | FEMS Microbiology Letters |
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croxfordunivpr:10.1093/femsle/fnz218 2024-09-09T19:21:32+00:00 Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp VuThi, Hai Jang, Sei-Heon Lee, ChangWoo Daegu University Research Grant 2019 http://dx.doi.org/10.1093/femsle/fnz218 http://academic.oup.com/femsle/advance-article-pdf/doi/10.1093/femsle/fnz218/30194884/fnz218.pdf https://academic.oup.com/femsle/article-pdf/366/18/fnz218/42816832/fnz218.pdf en eng Oxford University Press (OUP) https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model FEMS Microbiology Letters volume 366, issue 18 ISSN 0378-1097 1574-6968 journal-article 2019 croxfordunivpr https://doi.org/10.1093/femsle/fnz218 2024-06-24T04:24:11Z ABSTRACT Glutathione reductase is an important oxidoreductase that helps maintain redox homeostasis by catalyzing the conversion of glutathione disulfide to glutathione using NADPH as a cofactor. In this study, we cloned and characterized a glutathione reductase (hereafter referred to as SpGR) from Sphingomonas sp. PAMC 26621, an Arctic bacterium. SpGR comprises 449 amino acids, and functions as a dimer. Surprisingly, SpGR exhibits characteristics of thermophilic enzymes, showing optimum activity at 60°C and thermal stability up to 70°C with ∼50% residual activity at 70°C for 2 h. The amino acid composition analysis of SpGR showed a 1.9-fold higher Arg content (6%) and a 2.7-fold lower Lys/Arg ratio (0.75) compared to the Arg content (3.15%) and the Lys/Arg ratio (2.01) of known psychrophilic glutathione reductases. SpGR also exhibits its activity at 4°C, and circular dichroism and fluorescence spectroscopy results indicate that SpGR maintains its secondary and tertiary structures within the temperature range of 4–70°C. Taken together, the results of this study indicate that despite its origin from a psychrophilic bacterium, SpGR has high thermal stability. Our study provides an insight into the role of glutathione reductase in maintaining the reducing power of an Arctic bacterium in a broad range of temperatures. Article in Journal/Newspaper Arctic Oxford University Press Arctic FEMS Microbiology Letters |
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Open Polar |
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Oxford University Press |
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croxfordunivpr |
language |
English |
description |
ABSTRACT Glutathione reductase is an important oxidoreductase that helps maintain redox homeostasis by catalyzing the conversion of glutathione disulfide to glutathione using NADPH as a cofactor. In this study, we cloned and characterized a glutathione reductase (hereafter referred to as SpGR) from Sphingomonas sp. PAMC 26621, an Arctic bacterium. SpGR comprises 449 amino acids, and functions as a dimer. Surprisingly, SpGR exhibits characteristics of thermophilic enzymes, showing optimum activity at 60°C and thermal stability up to 70°C with ∼50% residual activity at 70°C for 2 h. The amino acid composition analysis of SpGR showed a 1.9-fold higher Arg content (6%) and a 2.7-fold lower Lys/Arg ratio (0.75) compared to the Arg content (3.15%) and the Lys/Arg ratio (2.01) of known psychrophilic glutathione reductases. SpGR also exhibits its activity at 4°C, and circular dichroism and fluorescence spectroscopy results indicate that SpGR maintains its secondary and tertiary structures within the temperature range of 4–70°C. Taken together, the results of this study indicate that despite its origin from a psychrophilic bacterium, SpGR has high thermal stability. Our study provides an insight into the role of glutathione reductase in maintaining the reducing power of an Arctic bacterium in a broad range of temperatures. |
author2 |
Daegu University Research Grant |
format |
Article in Journal/Newspaper |
author |
VuThi, Hai Jang, Sei-Heon Lee, ChangWoo |
spellingShingle |
VuThi, Hai Jang, Sei-Heon Lee, ChangWoo Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
author_facet |
VuThi, Hai Jang, Sei-Heon Lee, ChangWoo |
author_sort |
VuThi, Hai |
title |
Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
title_short |
Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
title_full |
Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
title_fullStr |
Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
title_full_unstemmed |
Cloning and characterization of a thermostable glutathione reductase from a psychrophilic Arctic bacterium Sphingomonas sp |
title_sort |
cloning and characterization of a thermostable glutathione reductase from a psychrophilic arctic bacterium sphingomonas sp |
publisher |
Oxford University Press (OUP) |
publishDate |
2019 |
url |
http://dx.doi.org/10.1093/femsle/fnz218 http://academic.oup.com/femsle/advance-article-pdf/doi/10.1093/femsle/fnz218/30194884/fnz218.pdf https://academic.oup.com/femsle/article-pdf/366/18/fnz218/42816832/fnz218.pdf |
geographic |
Arctic |
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Arctic |
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Arctic |
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Arctic |
op_source |
FEMS Microbiology Letters volume 366, issue 18 ISSN 0378-1097 1574-6968 |
op_rights |
https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model |
op_doi |
https://doi.org/10.1093/femsle/fnz218 |
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FEMS Microbiology Letters |
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1809761754039713792 |