l-Asparaginase II of Saccharomyces cerevisiae
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The activity profile of the periplasmic asparaginase of Saccharomyces cerevisiae was determined during cell growth in an ure2 mutant; in an ure2 transformed with a plasmid containing the gene URE2 and, for comparison, in the strain D273-10B. Cells were cultivated in media presenting variable quantitative and qualitative nitrogen availability and the enzyme activity was evaluated in fresh and in nitrogen-starved cells. Nitrogen affected the asparaginase II level in fresh and starved cells of all strains. In the best condition, enzyme was produced by the wild-type cells at the late log-phase in the glucose/ammonium medium with a carbon to nitrogen ratio 4.3:1. Upon starvation, the activity doubled. The overall profile of the transformed strain was similar to that of the wild-type strain. In the ure2 mutant, highenzyme levels were observed during growth, as expected. However the activity level, upon starvation, in proline grown cells, increased sixfold, suggesting that in addition to the Ure2p-Gln3p system, another system regulates asparaginase II biosynthesis.
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- l-Asparaginase II of Saccharomyces cerevisiae
Applied Biochemistry and Biotechnology
Volume 77, Issue 1-3 , pp 311-316
- Cover Date
- Print ISSN
- Online ISSN
- Humana Press
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- Saccharomyces cerevisiae
- URE2 protein
- nitrogen regulation
- l-asparaginase II
- nitrogen nutrition
- Industry Sectors
- Author Affiliations
- 1. Departmento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, 22949-900, Rio de Janeiro, R. J., Brazil
- 2. Departmento de Biologia Celular e Genética, Instituto de Biologia, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, Brazil