L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

Jones, Gary E.

doi:10.2172/4145400

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D-glucose1

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1973

1980

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Cited by 4 publications

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References 33 publications

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“…Concurrent with the above determinations, the strain-specific asparaginase activities of various yeast strains were observed in the presence of para-hydroxymercuribenzoate (p-OHMB). It had been reported previously that p-OHMB caused a partial inhibition (56%) of yeast asparaginase (6). The data (Table 5) show a distinct difference between individual strain responses.…”

Section: D-glucosesupporting

confidence: 63%

L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme

Dunlop

Roon²

1975

J Bacteriol

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During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an extemally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibtion, whereas the internal activity is highly inhibited by this compound.

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Section: D-glucosesupporting

confidence: 63%