The effect of tryptophan analogs on the induced synthesis of maltase and protein synthesis in yeast

Abstract

Previous studies (l-3) on the induced synthesis of cr-glucosidase in nondividing suspensions of Saccharomyces cerevisiae have indicated that the process involves the de nova formation of protein from the free amino acid pool. The data led to the conclusion that the first stable intermediate between the free amino acids and the fully formed enzyme molecule was of such complexity that its synthesis demanded the simultaneous availability of virtually all the various free amino acid pool components. Much of the information obtained in the course of these studies stems principally from the use of halogenated derivatives of phenylalanine. In view of the importance of the conclusions drawn, it was of interest to subject them to further tests with effective analogs of other amino acids. In looking for utilizable antagonists, two principles were kept in mind. The compounds should be analogs of free amino acid pool components which are present in relatively low concentrations. Further, it should be possible to demonstrate the existence of a competitive interaction with the corresponding homologs. The results reported in the present paper