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The enzymes of ammonia assimilation in Schizosaccharomyces spp. and in Saccharomycodes ludwigii.

The assimilation of ammonia in many yeasts is mediated by NADP-linked glutamate dehydrogenase. The synthesis of this enzyme appears to be derepressed during growth in environments containing low concentrations of ammonia or, as in Candida utilis, where nitrate is the nitrogen source (Brown & Johnson, 1970; Burn, Turner & Brown, 1974). An alternative pathway, common in bacteria (Tempest, Meers & Brown, I 973) , involves the enzymes glutamine synthetase and glutamate synthase. Glutamine synthetase is widespread in yeasts, while glutamate synthase has been detected in certain Schizosaccharomyces spp. (Brown, Burn & Johnson, 1973). Roon, Even & Larimore (1974) have reported the presence of glutamate synthase in some strains of Saccharomyces cerevisiae, together with much higher levels of both NADand NADP-linked glutamate dehydrogenase. We report the results of chemostat studies on the levels of enzymes involved in ammonia assimilation in representatives of the four recognized (Lodder, 1970) species of the genus Schizosaccharomyces and the single recognized species of the related genus Saccharomy codes.