Identification of the Cysteine Residues Involved in Redox Modification of Plant Plastidic Glucose-6-phosphate Dehydrogenase

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This work aims to identify the specific cysteine residues in plastidic G6PDH that are involved in redox regulation.
Modified cDNA sequences encoding G6PDH from potato were overexpressed in Escherichia coli.
Site-directed mutagenesis was performed to replace cysteine residues with serine to assess redox sensitivity.
Characterization of enzyme activity was conducted post-reduction with agents such as dithiothreitol and glutathione.
Cys149 and Cys157 mutants exhibited characteristics of the reduced wild-type enzyme, indicating their role in regulation.
Inactivation of wild-type plastidic G6PDH could be reversed by oxidants, while cytosolic isoenzyme remained unaffected.
The plastidic enzyme showed redox regulation through thioredoxin m, highlighting differences between isoforms.

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Identifies cysteine residues critical for redox regulation of plastidic G6PDH in plants, suggesting key regulatory mechanisms.

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Wenderoth et al. (1997) studied this question.

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