NDLI: Two GPX-like proteins fromLycopersicon esculentumandHelianthus annuusare antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities

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Two GPX-like proteins fromLycopersicon esculentumandHelianthus annuusare antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities

Content Provider	Scilit
Author	Herbette, Stéphane Lenne, Catherine Leblanc, Nathalie Julien, Jean-Louis Drevet, Joël R. Roeckel-Drevet, Patricia
Copyright Year	2002
Description	Journal: Journal of Biological Inorganic Chemistry This study investigated the enzymatic function of two putative plant GPXs, GPXle1 from Lycopersicon esculentum and GPXha2 from Helianthus annuus, which show sequence identities with the mammalian phospholipid hydroperoxide glutathione peroxidase (PHGPX). Both purified recombinant proteins expressed in Escherichia coli show PHGPX activity by reducing alkyl, fatty acid and phospholipid hydroperoxides but not hydrogen peroxide in the presence of glutathione. Interestingly, both recombinant GPXle1 and GPXha2 proteins also reduce alkyl, fatty acid and phospholipid hydroperoxides as well as hydrogen peroxide using thioredoxin as reducing substrate. Moreover, thioredoxin peroxidase (TPX) activities were found to be higher than PHGPX activities in terms of efficiency and substrate affinities, as revealed by their respective $V_{max}$ and $K_{m}$ values. We therefore conclude that these two plant GPX-like proteins are antioxidant enzymes showing PHGPX and TPX activities.
Ending Page	2420
Starting Page	2414
ISSN	2573508X
e-ISSN	14321327
DOI	10.1046/j.1432-1033.2002.02905.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	9
Volume Number	269
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2002-04-22
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biotechnology and Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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