2000
DOI: 10.1146/annurev.arplant.51.1.371
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Abstract: s Abstract Thioredoxins, the ubiquitous small proteins with a redox active disulfide bridge, are important regulatory elements in plant metabolism. Initially recognized as regulatory proteins in the reversible light activation of key photosynthetic enzymes, they have subsequently been found in the cytoplasm and in mitochondria. The various plant thioredoxins are different in structure and function. Depending on their intracellular location they are reduced enzymatically by an NADP-dependent or by a ferredoxin … Show more

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Cited by 370 publications
(270 citation statements)
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“…The proteins identified in the present study function in a spectrum of chloroplast processes (Table 2). In addition to FBPase, four other enzymes of the Calvin cycle, all known targets, showed an electrostatic interaction with thioredoxin -glyceraldehyde 3-phosphate dehydrogenase, rubisco activase, rubisco small subunit and transketolase (Schürmann and Jacquot 2000;Motohashi et al 2001;Balmer et al 2003). These enzymes function in the three phases of the Calvin cycle: carboxylation, reduction and regeneration.…”
Section: Resultsmentioning
confidence: 99%
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“…The proteins identified in the present study function in a spectrum of chloroplast processes (Table 2). In addition to FBPase, four other enzymes of the Calvin cycle, all known targets, showed an electrostatic interaction with thioredoxin -glyceraldehyde 3-phosphate dehydrogenase, rubisco activase, rubisco small subunit and transketolase (Schürmann and Jacquot 2000;Motohashi et al 2001;Balmer et al 2003). These enzymes function in the three phases of the Calvin cycle: carboxylation, reduction and regeneration.…”
Section: Resultsmentioning
confidence: 99%
“…These enzymes function in the three phases of the Calvin cycle: carboxylation, reduction and regeneration. The other newly identified proteins found to associate with thioredoxin f include known targets functional in a number of chloroplast processes: translation (28 kDa ribonucleoprotein, elongation factor tu and ribosomal protein S30); protein assembly/folding (70 kDa heat shock protein and rubisco binding protein); C 4 /malate valve (malate dehydrogenase); ATP synthesis (ATP synthase gamma subunit); nitrogen metabolism (glutamine synthetase); tetrapyrrole biosynthesis (glutamate-1-semialdehyde 2,1 aminomutase); fatty acid biosynthesis (acetyl-CoA carboxylase); starch biosynthesis (ADP-glucose pyrophosphorylase); protein degradation (ATP dependent clp protease) and HCO 3 − /CO 2 equilibration (carbonic anhydrase) (Schürmann and Jacquot 2000;Balmer et al 2003).…”
Section: Resultsmentioning
confidence: 99%
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“…The highly conserved active site, Trp-Cys-Gly-Pro-Cys, contains a disulphide group that undergoes reversible redox changes between S-S and 2SH (Ruelland andMiginiac-Maslow 1999, Sch rmann andJacquot 2000). Thioredoxins serve as electron donors in a variety of cellular redox reactions.…”
Section: Light Activation By Thioredoxinsmentioning
confidence: 99%
“…Also some chloroplast-located enzymes involved in nitrogen metabolism are activated by thioredoxins, i.e. glutamine synthetase, ferredoxin-dependent glutamate synthase, and the first enzyme in the pathway of aromatic amino acids (Ruelland andMiginiac-Maslow 1999, Sch rmann andJacquot 2000).…”
Section: Light Activation By Thioredoxinsmentioning
confidence: 99%