Abstract
Ammonium ions inactivate the basic amino acid transport system in Schizosaccharomyces pombe in an irreversible manner. The inactivation is accompanied by a 4-fold decrease of K T of l-lysine transport, leaving its J max unchanged; phenylmethylsulfonyl fluoride protects the system against inactivation. In contrast, two basic amino acid transport systems in a gap1 mutant of Saccharomyces cerevisiae are influenced by NH 4 + ions in such a way that only the J max decreases while the K T of l-lysine transport is unchanged. Phenylmethylsulfonyl fluoride does not act here as a protective agent.
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