%0 Journal Article %A Cossar, J. D. %A Rowell, P. %A Stewart, W. D. P. %T Thioredoxin as a Modulator of Glucose-6-phosphate Dehydrogenase in a N2-Fixing Cyanobacterium %D 1984 %J Microbiology, %V 130 %N 4 %P 991-998 %@ 1465-2080 %R https://doi.org/10.1099/00221287-130-4-991 %I Microbiology Society, %X Glucose-6-phosphate dehydrogenase (G6PDH) is a key enzyme involved in fixed carbon dissimilation in photosynthetic micro-organisms; in heterocystous cyanobacteria it may also be implicated in the supply of reductant to nitrogenase. In crude cell-free extracts of the N2-fixing cyanobacterium Anabaena variabilis G6PDH activity was reversibly deactivated by the thiol agent dithiothreitol in the presence of a low molecular weight protein (12000mol. wt). Glucose 6-phosphate reversed deactivation when added at high concentration, or prevented deactivation if added with the thiol. NADP+, which, like glucose 6-phosphate, is a G6PDH substrate, also deactivated the enzyme; deactivation was reversed or prevented by adding glucose 6-phosphate or glutamine. Purified thioredoxin from Anabaena cylindrica, at very low concentrations (2 nm), deactivated purified G6PDH in a manner identical to that observed when crude extracts were used in the presence of dithiothreitol. Glutathione did not affect the enzyme. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-130-4-991