Inhibition of nitrate utilization by amino acids in intact Anacystis nidulans cells.

In an attempt to establish the nature of the ammonium-assimilation products which mediate the inhibition by ammonium of nitrate uptake in cyanobacteria, the effect of different amino acids on nitrate utilization by intact Anacystis nidulans cells has been assayed. To exclude an indirect inhibition of nitrate uptake through the ammonium which the amino acids might release, the cells were pretreated with L-methionine-D,L-sulfoximine (MSX), a potent inactivator of glutamine synthetase. Under these conditions, several L-amino acids, but not the corresponding D-isomers, affected nitrate utilization to a variable extent, causing inhibitions ranging between 20 and 80% when added at 20 mM concentration. For most of the inhibitory amino acids, including L-isoleucine, L-leucine and L-valine, a correlation was found between their ability to act as amino group donors to alpha-ketoglutarate, in reactions catalyzed by A. nidulans cell-free extracts, and their inhibitory effect on nitrate utilization. L-Glutamine, L-asparagine and glycine, being effective inhibitors of nitrate utilization, were poor substrates for the transaminating activity to alpha-ketoglutarate, however. The possible role of the latter amino acids as mediators in the ammonium-promoted inhibition of nitrate uptake is discussed.