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  4. Heterodimer formation between thioredoxin <i>f</i> and fructose 1,6-bisphosphatase from spinach chloroplasts
 
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Heterodimer formation between thioredoxin <i>f</i> and fructose 1,6-bisphosphatase from spinach chloroplasts

Auteur(s)
Balmer, Yves
Editeur(s)
Schürmann, Peter
Date de parution
2001
In
FEBS Letters, Elsevier, 2001/492/1-2/58-61
Mots-clés
  • Spinach

  • Fructose 1

  • 6-Bisphosphatase

  • Thioredoxin <i>f</i>

  • Site-directed mutagen...

  • Intermolecular disulf...

  • Heterodimer

Résumé
Chloroplast fructose 1,6-bisphosphatase (FBPase) is activated by reduction of a regulatory disulfide through thioredoxin <i>f</i> (Trx f). In the course of this reduction a transient mixed disulfide is formed linking covalently Trx <i>f</i> with FBPase, which possesses three Cys on a loop structure, two of them forming the redox-active disulfide bridge. The goal of this study was to identify the Cys involved in the transient mixed disulfide. To stabilize this reaction intermediate, mutant proteins with modified active sites were used. We identified Cys-155 of the FBPase as the one engaged in the formation of the mixed disulfide intermediate with Cys-46 of Trx <i>f</i>.
URI
https://libra.unine.ch/handle/123456789/15377
DOI
10.1016/S0014-5793(01)02229-3
Autre version
http://dx.doi.org/10.1016/S0014-5793(01)02229-3
Type de publication
Resource Types::text::journal::journal article
Dossier(s) à télécharger
 main article: Sch_rmann_Peter_-_Heterodimer_formation_between_20090515.pdf (394.84 KB)
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