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Saccharomyces cerevisiae X2180-1A synthesizes two forms of asparaginase: L-asparaginase I, an internal constitutive enzyme, and asparaginase II, an external enzyme which is secreted in response to nitrogen starvation. The two enzymes are biochemically and genetically distinct. The structural gene for asparaginase I (asp 1) is closely linked to the trp 4(More)
Detailed kinetic analysis was performed on asparaginase II, a cell wall glycoprotein from Saccharomyces cerevisiae. The enzyme was highly active in the hydrolysis and hydroxylaminolysis reactions with D- and L-asparagine and with a variety of N-substituted analogues. The data from studies involving pH dependencey, substrate saturation, and product(More)
Two lines of evidence suggest that amino acid transport systems and the methylamine/ammonia transport system of Saccharomyces cerevisiae may share a common component or components. 1. Mutant strains have been derived which are defective in transport activity for methylamine and for amino acids. A single pleiotropic mutation appears to be responsible for the(More)
The biosynthesis of asparaginase II in Saccharomyces cerevisiae is subject to strong catabolite repression by a variety of nitrogen compounds. In the present study, asparaginase II synthesis was examined in a wild-type yeast strain and in strains carrying gdhA, gdhCR, or gdhCS mutations. The following effects were observed: (i) In the wild-type strain, the(More)
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