Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions.
Identifieur interne : 000A55 ( Main/Exploration ); précédent : 000A54; suivant : 000A56Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions.
Auteurs : Xing-Huang Gao [France] ; Mirko Zaffagnini ; Mariette Bedhomme ; Laure Michelet ; Corinne Cassier-Chauvat ; Paulette Decottignies ; Stéphane D. LemaireSource :
- FEBS letters [ 1873-3468 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Chlamydomonas reinhardtii, Cystéine, Disulfures, Glutarédoxines.
- Catalyse, Cinétique, Sensibilité et spécificité.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cysteine, Disulfides, Glutaredoxins.
- metabolism : Chlamydomonas reinhardtii.
- Catalysis, Kinetics, Sensitivity and Specificity.
Abstract
Protein deglutathionylation is mainly catalyzed by glutaredoxins (GRXs). We have analyzed the biochemical properties of four of the six different GRXs of Chlamydomonas reinhardtii. Kinetic parameters were determined for disulfide and dehydroascorbate reduction but also for deglutathionylation of artificial and protein substrates. The results indicate that GRXs exhibit striking differences in their catalytic properties, mainly linked to the class of GRX considered but also to the pK(a) of the N-terminal catalytic cysteine. Furthermore, glutathionylated proteins were found to exhibit distinct reactivities with GRXs. These results suggest that glutathionylation may allow a fine tuning of cell metabolism under stress conditions.
DOI: 10.1016/j.febslet.2010.04.034
PubMed: 20406640
Affiliations:
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We have analyzed the biochemical properties of four of the six different GRXs of Chlamydomonas reinhardtii. Kinetic parameters were determined for disulfide and dehydroascorbate reduction but also for deglutathionylation of artificial and protein substrates. The results indicate that GRXs exhibit striking differences in their catalytic properties, mainly linked to the class of GRX considered but also to the pK(a) of the N-terminal catalytic cysteine. Furthermore, glutathionylated proteins were found to exhibit distinct reactivities with GRXs. 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We have analyzed the biochemical properties of four of the six different GRXs of Chlamydomonas reinhardtii. Kinetic parameters were determined for disulfide and dehydroascorbate reduction but also for deglutathionylation of artificial and protein substrates. The results indicate that GRXs exhibit striking differences in their catalytic properties, mainly linked to the class of GRX considered but also to the pK(a) of the N-terminal catalytic cysteine. Furthermore, glutathionylated proteins were found to exhibit distinct reactivities with GRXs. These results suggest that glutathionylation may allow a fine tuning of cell metabolism under stress conditions.</AbstractText><CopyrightInformation>Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. 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Lemaire</name><name sortKey="Michelet, Laure" sort="Michelet, Laure" uniqKey="Michelet L" first="Laure" last="Michelet">Laure Michelet</name><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name></noCountry><country name="France"><noRegion><name sortKey="Gao, Xing Huang" sort="Gao, Xing Huang" uniqKey="Gao X" first="Xing-Huang" last="Gao">Xing-Huang Gao</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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