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Ammonium Assimilation by Candida albicans and Other Yeasts: Evidence for Activity of Glutamate Synthase

By R. Holmes, Alan Collings, Kevin J. F. Farnden and Maxwell G. Shepherd


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

Year: 1989
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