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Aspartate kinase and homoserine dehydrogenase ofCandida utilis

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Abstract

Aspartate kinase and homoserine dehydrogenase activity were assayed in a dialyzed cell-free extract ofCandida utilis. Aspartate kinase was partly inhibited by ATP-Mg and by Mg2+ alone. There appear to be two isoenzymes of aspartate kinase in the yeast, one heatlabile, the other relatively heat-stable. The first is subject to feedback inhibition by threonine, the other is threonine-resistant. Neither aspartate kinase nor homoserine dehydrogenase is the rate-limiting enzyme in methionine biosynthesis. Homoserine dehydrogenase measured in the forward direction showed an activity five times higher than aspartate kinase. No regulatory interaction could be demonstrated for this enzyme. No repression of aspartate kinase and homoserine dehydrogenase synthesis by threonine, methionine or both amino acids was observed.

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Authors and Affiliations

  1. Department of Molecular Genetics, Centro Nacional de Investigaciones Cientificas, P.O. Box 6990, La Habana, Cuba

    J. A. Benítez, J. M. Delgado & L. S. Herrera

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  1. J. A. Benítez
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  2. J. M. Delgado
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  3. L. S. Herrera
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Benítez, J.A., Delgado, J.M. & Herrera, L.S. Aspartate kinase and homoserine dehydrogenase ofCandida utilis . Folia Microbiol 28, 149–156 (1983). https://doi.org/10.1007/BF02884077

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  • DOI: https://doi.org/10.1007/BF02884077

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