Abstract
Only a single l-asparaginase has been found in the yeast Saccharomyces cerevisiae. The enzyme is synthesized constitutively, and its functioning is not controlled by the products of its activity. The apparent Km for the yeast l-asparaginase reaction is 2.5×10−4 m. Activity is greatest at pH 8.5 and is unaffected by the ionic strength of reaction mixtures. l-Asparagine can serve as the sole nitrogen source for cell metabolism but cannot serve as the sole supply of carbon. Active l-asparaginase is necessary for the use of l-asparagine as a nitrogen donor for cell growth. This requirement suggests a possible way in which l-asparaginase-deficient strains of yeast or other organisms might easily be selected.
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G.E.J. was supported by U.S. Public Health Service Predoctoral Fellowship No. 5 F01 GM36,437.
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Jones, G.E., Mortimer, R.K. Biochemical properties of yeast l-asparaginase. Biochem Genet 9, 131–146 (1973). https://doi.org/10.1007/BF00487443
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DOI: https://doi.org/10.1007/BF00487443