L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme

Dunlop, P. C.; Roon, Robert J.

doi:10.1128/jb.122.3.1017-1024.1975

Cited by 70 publications

(43 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Alternatively, there may be multiple oxidases. The intracellular and extracellular oxidases may differ in a manner similar to that of the asparaginases of S. cerevisiae (9,13), or each oxidase may be distinct from all other oxidases, irrespective of its intracellular or extracellular nature. Such possibilities are readily amenable to biochemical and genetic dissection, which will allow us to compare directly the oxidases produced under the various conditions that have now been reported.…”

Section: Methodsmentioning

confidence: 99%

Participation of an extracellular deaminase in amino acid utilization by Neurospora crassa

DeBusk¹,

Ogilvie²

1984

J Bacteriol

View full text Add to dashboard Cite

A strain of Neurospora crassa defective in amino acid transport can utilize a variety of amino acids for growth when readily metabolizable nitrogen is limiting. Growth is accompanied by the production of an extracellular deaminase that converts the amino acid to its respective keto acid plus equimolar quantities of utilizable nitrogen in the ammonium ion form. Production of the deaminase is subject to ammonium repression. The relationship between the ability of an amino acid to trigger deaminase production and the presence of particular amino acid permease deficiencies is complex. Four classes of amino acids have been defined with respect to this relationship. The existence of multiple extracellular deaminases is discussed.

show abstract

Section: Methodsmentioning

confidence: 99%

Participation of an extracellular deaminase in amino acid utilization by Neurospora crassa

DeBusk¹,

Ogilvie²

1984

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Cell debris was removed by centrifugation (5 min at 7500 g). The supernatant was immediately used to assay asparaginase activity, as described by Dunlop & Roon (1975).…”

Section: Asparaginase Assaymentioning

confidence: 99%

Single QTL mapping and nucleotide-level resolution of a physiologic trait in wineSaccharomyces cerevisiaestrains

Marullo¹,

Aigle²,

Bely³

et al. 2007

FEMS Yeast Research

View full text Add to dashboard Cite

Natural Saccharomyces cerevisiae yeast strains exhibit very large genotypic and phenotypic diversity. However, the link between phenotype variation and genetic determinism is still difficult to identify, especially in wild populations. Using genome hybridization on DNA microarrays, it is now possible to identify single-feature polymorphisms among divergent yeast strains. This tool offers the possibility of applying quantitative genetics to wild yeast strains. In this instance, we studied the genetic basis for variations in acetic acid production using progeny derived from two strains from grape must isolates. The trait was quantified during alcoholic fermentation of the two strains and 108 segregants derived from their crossing. A genetic map of 2212 markers was generated using oligonucleotide microarrays, and a major quantitative trait locus (QTL) was mapped with high significance. Further investigations showed that this QTL was due to a nonsynonymous single-nucleotide polymorphism that targeted the catalytic core of asparaginase type I (ASP1) and abolished its activity. This QTL was only effective when asparagine was used as a major nitrogen source. Our results link nitrogen assimilation and CO(2) production rate to acetic acid production, as well as, on a broader scale, illustrating the specific problem of quantitative genetics when working with nonlaboratory microorganisms.

show abstract

“…L-Asparaginase I, which is constitutive and is coded for by a single structural gene (7,10,11), appears to interact primarily with intracellular pools of L-asparagine, perhaps functioning as a part of a mechanism by which these pools are controlled. Asparaginase II, which is derepres-sible by nitrogen starvation and requires tunctional product of at least two genes (3,4,8,9), apparently functions either as a sensor/effector related to the state of nitrogen metabolism in the cell or as an element that responds to a separate sensor of nitrogen balance in the cell. Almost certainly, these regulatory mechanisms will involve the cells' ability to synthesize Lasparagine and thereby convert nitrogen into the amide form.…”

mentioning

confidence: 99%

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

Jones¹

1978

J Bacteriol

View full text Add to dashboard Cite

L-Asparagine auxotrophy in Saccharomyces cerevisiae is the result of mutation in each of two unlinked cistrons, ASN1 and ASN2. Mutation in only one of these cistrons yields growth indistinguishable from that of wild-type cells under a variety of nutritional stresses. Relatively high concentrations of L-asparagine are required to permit maximal growth of the auxotrophs, and the amino acid requirement cannot be satisfied by a variety of other amino acids that serve as nitrogen sources for cell growth. Although reversion of the mutations can occur, haploid populations of cells containing only low frequencies of prototrophs can be maintained easily. In diploid cells heteroallelic for certain combinations of alleles of the two genes, mitotic recombination gives rise to prototrophic cells that accumulate to high frequency in populations of the cells.

show abstract

L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme

Cited by 70 publications

References 12 publications

Participation of an extracellular deaminase in amino acid utilization by Neurospora crassa

Participation of an extracellular deaminase in amino acid utilization by Neurospora crassa

Single QTL mapping and nucleotide-level resolution of a physiologic trait in wineSaccharomyces cerevisiaestrains

L-Asparagine auxotrophs of Saccharomyces cerevisiae: genetic and phenotypic characterization

Contact Info

Product

Resources

About