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Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica
The parasitic helminth Fasciola hepatica secretes a 2-Cys peroxiredoxin (Prx) that may play important functions in host–parasite interaction. Recombinant peroxiredoxin (FhePrx) prevented metal-catalyzed oxidative nicking of plasmid DNA and detoxified hydrogen peroxide when coupled with Escherichia c...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Federation of European Biochemical Societies. Published by Elsevier B.V.
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127579/ https://www.ncbi.nlm.nih.gov/pubmed/16938293 http://dx.doi.org/10.1016/j.febslet.2006.08.019 |
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author | Sekiya, Mary Mulcahy, Grace Irwin, Jane A. Stack, Colin M. Donnelly, Sheila M. Xu, Weibo Collins, Peter Dalton, John P. |
author_facet | Sekiya, Mary Mulcahy, Grace Irwin, Jane A. Stack, Colin M. Donnelly, Sheila M. Xu, Weibo Collins, Peter Dalton, John P. |
author_sort | Sekiya, Mary |
collection | PubMed |
description | The parasitic helminth Fasciola hepatica secretes a 2-Cys peroxiredoxin (Prx) that may play important functions in host–parasite interaction. Recombinant peroxiredoxin (FhePrx) prevented metal-catalyzed oxidative nicking of plasmid DNA and detoxified hydrogen peroxide when coupled with Escherichia coli thioredoxin and thioredoxin reductase (k(cat)/K(m) = 5.2 × 10(5) M(−1) s(−1)). Enzyme kinetic analysis revealed that the catalytic efficiency of FhePrx is similar to other 2-Cys peroxiredoxins; the enzyme displayed saturable enzyme Michaelis–Menten type kinetics with hydrogen peroxide, cumene hydroperoxide and t-butyl hydroperoxide, and is sensitive to concentrations of hydrogen peroxide above 0.5 mM. Like the 2-Cys peroxiredoxins from a related helminth, Schistosoma mansoni, steady-state kinetics indicate that FhePrx exhibits a saturable, single displacement-like reaction mechanism rather than non-saturable double displacement (ping–pong) enzyme substitution mechanism common to other peroxiredoxins. However, unlike the schistosome Prxs, FhePrx could not utilise reducing equivalents supplied by glutathione or glutathione reductase. |
format | Online Article Text |
id | pubmed-7127579 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Federation of European Biochemical Societies. Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71275792020-04-06 Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica Sekiya, Mary Mulcahy, Grace Irwin, Jane A. Stack, Colin M. Donnelly, Sheila M. Xu, Weibo Collins, Peter Dalton, John P. FEBS Lett Article The parasitic helminth Fasciola hepatica secretes a 2-Cys peroxiredoxin (Prx) that may play important functions in host–parasite interaction. Recombinant peroxiredoxin (FhePrx) prevented metal-catalyzed oxidative nicking of plasmid DNA and detoxified hydrogen peroxide when coupled with Escherichia coli thioredoxin and thioredoxin reductase (k(cat)/K(m) = 5.2 × 10(5) M(−1) s(−1)). Enzyme kinetic analysis revealed that the catalytic efficiency of FhePrx is similar to other 2-Cys peroxiredoxins; the enzyme displayed saturable enzyme Michaelis–Menten type kinetics with hydrogen peroxide, cumene hydroperoxide and t-butyl hydroperoxide, and is sensitive to concentrations of hydrogen peroxide above 0.5 mM. Like the 2-Cys peroxiredoxins from a related helminth, Schistosoma mansoni, steady-state kinetics indicate that FhePrx exhibits a saturable, single displacement-like reaction mechanism rather than non-saturable double displacement (ping–pong) enzyme substitution mechanism common to other peroxiredoxins. However, unlike the schistosome Prxs, FhePrx could not utilise reducing equivalents supplied by glutathione or glutathione reductase. Federation of European Biochemical Societies. Published by Elsevier B.V. 2006-09-18 2006-08-22 /pmc/articles/PMC7127579/ /pubmed/16938293 http://dx.doi.org/10.1016/j.febslet.2006.08.019 Text en Copyright © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Sekiya, Mary Mulcahy, Grace Irwin, Jane A. Stack, Colin M. Donnelly, Sheila M. Xu, Weibo Collins, Peter Dalton, John P. Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title | Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title_full | Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title_fullStr | Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title_full_unstemmed | Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title_short | Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica |
title_sort | biochemical characterisation of the recombinant peroxiredoxin (fheprx) of the liver fluke, fasciola hepatica |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127579/ https://www.ncbi.nlm.nih.gov/pubmed/16938293 http://dx.doi.org/10.1016/j.febslet.2006.08.019 |
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