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Redox regulation of chloroplastic glucose‐6‐phosphate dehydrogenase: A new role for f‐type thioredoxin
Author(s) -
Née Guillaume,
Zaffagnini Mirko,
Trost Paolo,
Issakidis-Bourguet Emmanuelle
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.035
Subject(s) - pentose phosphate pathway , dehydrogenase , biochemistry , oxidative phosphorylation , thioredoxin , ferredoxin , glucose 6 phosphate dehydrogenase , enzyme , glycolysis , gene isoform , chemistry , biology , gene
Glucose‐6‐phosphate dehydrogenase (G6PDH) is the key enzyme of the oxidative pentose phosphate pathway supplying reducing power (as NADPH) in non‐photosynthesizing cells. We have examined in detail the redox regulation of the plastidial isoform predominantly present in Arabidopsis green tissues (AtG6PDH1) and found that its oxidative activation is strictly dependent on plastidial thioredoxins (Trxs) that show differential efficiencies. Light/dark modulation of AtG6PDH1 was reproduced in vitro in a reconstituted ferredoxin/Trx system using f‐type Trx allowing to propose a new function for this Trx isoform co‐ordinating both reductive (Calvin cycle) and oxidative pentose phosphate pathways.