Activities and properties of the ammonium assimilation enzymes NADP+-dependent glutamate dehydrogenase (GDH), glutamate synthase (GOGAT) and glutamine synthetase (GS) were determined in batch and continuous cultures of Candida albicans. NADP+-dependent GDH activity showed allosteric kinetics, with an So.s for 2-oxoglutarate of 7.5 mM and an apparent K , for ammonium of 5-0 mM. GOGAT activity was affected by the buffer used for extraction and assay, but in phosphate buffer, kinetics were hyperbolic, yielding K , values for glutamine of 750 p~ and for 2-oxoglutarate of 65 p~. The enzymes GOGAT and NADP+-dependent GDH were also assayed in batch cultures of Saccharomyces cerevisiae and three other pathogenic Candida spp. : Candida tropicalis, Candida pseudotropicalis and Candida parapsilosis. Evidence is presented that GSlGOGAT is a major pathway for ammonium assimilation in Candida albicans and that this pathway is also significant in other Candida species.