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In the light, plastidial G6PDH enzymes are inactivated by disulfidedithiol interchange of a redox-sensitive disulfide bridge (Scheibe, The two cysteine residues that are responsible for redox regulation of G6PDH activity in plastids were elucidated with recombinant enzymes from potato (P1 class, Wenderoth et al., m2 seems to play an additional role in alternative targeting of G6PD1 to peroxisomes, leading to cytosolic retention, which involves the catalytically inactive but evolutionary conserved G6PD4 isoform (Meyer et al., m2 (retained by an as yet unknown mechanism in the cytosol) binds as co-chaperon to plastidial OPPP precursors in the cytosol