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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
Schürmann, Peter 
Institut de biologie 
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 mutagenesis
  • Intermolecular disulfide
  • Heterodimer
  • 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>.
Identifiants
https://libra.unine.ch/handle/123456789/15377
_
10.1016/S0014-5793(01)02229-3
Type de publication
journal article
Dossier(s) à télécharger
 main article: Sch_rmann_Peter_-_Heterodimer_formation_between_20090515.pdf (394.84 KB)
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