Abstract
The present communication defines the conditions under which thioredoxin activates glutamine synthetase from Anabaena cylindrica. Effects are obtained at pH values around neutrality, and the activation is affected by Mg2+ in the assays. The thioredoxin systems from A. cylindrica and spinach are functionally interchangeable in the activation of glutamine synthetase. The enzyme is efficiently activated by thioredoxinm and also by thioredoxinf, but at much higher concentrations. Thioredoxinm has previously been shown to activate NADPH-dependent malate dehydrogenase and isocitrate dehydrogenase from cyanobacteria. It is speculated that thioredoxinm plays a role in the differentiation of vegetative cells to heterocysts.
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