The assay of yeast ureidoglycolatase

Choi, Kang-Duk; Lee, Katharine W.; Roush, Allan H.

doi:10.1016/0003-2697(66)90177-1

Cited by 17 publications

(7 citation statements)

References 14 publications

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“…Isolation and characterization of urea transport mutant strains. Ureidoglycolate has been reported to serve as a nitrogen source for several strains of bacteria and yeast (3,7,13,15). We also have observed growth of our wildtype strains using this compound as sole nitrogen source.…”

Section: Resultssupporting

confidence: 64%

Urea transport-defective strains of Saccharomyces cerevisiae

1976

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Experiments characterizing the urea active transport system in Saccharomyces cerevisiae indicate that (i) formamide and acetamide are strong competitive inhibitors of urea accumulation, (ii) uptake is maximal at pH 3.3 and is 80% inhibited at pH 6.0, and (iii) adenosine 5'-triphosphate generated by glycolysis in conjunction with formation of an ion gradient is likely the driving force behind urea transport. Mutant strains were isolated that are unable to accumulate urea at external concentrations of 0.25 mM. These strains also exhibit a depressed growth rate on 10 mM urea, indicating existence of a relationship between the active transport and facilitated diffusion modes of urea uptake. Urea transport in Saccharomyces cerevisiae may occur by two routes (5). The first mode is a

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Section: Resultssupporting

confidence: 64%

Urea transport-defective strains of Saccharomyces cerevisiae

1976

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“…If these two pathways are appropriately blocked, then the intracellular level of allophanate would decrease and a greater-fold increase in allan- Cultures of M-25 and M-62 were grown on minimal-ammonia medium in the presence or absence of 10 mM urea. At a cell density of 60 klett units, the cells were harvested and assayed for allantoicase and ureidoglycolate hydrolase (5,13). Enzyme activities are all expressed as nmol of glyoxylate produced per min per mg of soluble protein.…”

Section: Resultsmentioning

confidence: 99%

Induction of the Allantoin Degradative Enzymes in Saccharomyces cerevisiae by the Last Intermediate of the Pathway

Cooper¹,

Lawther

1973

Proc. Natl. Acad. Sci. U.S.A.

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Saccharomyces cerevisiae can degrade allantoin in five steps to glyoxylate, ammonia, and "CO2."We previously demonstrated that synthesis of the urea carboxylase-allophanate hydrolase multienzyme complex is contingent upon the presence of allophanic acid, the product of the urea carboxylase reaction. Since these enzymes catalyze the last two reactions of allantoin degradation, experiments were performed to establish whether or not the presence of allophanic acid was required for synthesis of any other enzymes participating in this degradative pathway. The data presented here indicate that allophanic acid is required for synthesis of all enzymes participating in allantoin degradation. This conclusion is based upon the observation that: (i) wild-type strains produced a large amount of allantoinase upon addition of allantoin, allantoate, ureidoglycolate, or urea to the medium, (ii) no increase in activity was observed unless the added compound could be metabolized to allophanate, (iii) strains lacking allophanate hydrolase contained large amounts of allantoinase even in the absence of added urea, and (iv) the urea analogue, formamide, was capable of inducing allantoinase synthesis in wild-type strains but would not serve this function in a strain lacking urea carboxylase.

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“…Allantoicase (DAL2) and ureidoglycolate hydrolase (DAL3) activities were measured as described previously (5,14). Transformed and untransformed S. cerevisiae cells were grown in 200 ml of Wickerham minimalglucose medium with glutamate (0.1%) provided as the sole nitrogen source.…”

Section: Methodsmentioning

confidence: 99%

Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae.

Yoo¹,

Genbauffe²,

Cooper³

1985

Mol. Cell. Biol.

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This report describes the isolation of the genes encoding allantoicase (DAL2) and ureidoglycolate hydrolase (DAL3), which are components of the large DAL gene cluster on the right arm of chromosome IX of Saccharomyces cerevisiae. During this work a new gene (DAL7) was identified and found to be regulated in the manner expected for an allantoin pathway gene. Its expression was (i) induced by allophanate, (ii) sensitive to nitrogen catabolite repression, and (iii) responsive to mutation of the DAL80 and DAL8J loci, which have previously been shown to regulate the allantoin degradation system. Hybridization probes generated from these cloned genes were used to analyze expression of the allantoin pathway genes in wild-type and mutant cells grown under a variety of physiological conditions. When comparison was possible, the patterns of mRNA and enzyme levels observed in various strains and physiological conditions were very similar, suggesting that the system is predominantly regulated at the level of gene expression. Although all of the genes seem to be controlled by a common mechanism, their detailed patterns of expression were, at the same time, highly individual and diverse.

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The assay of yeast ureidoglycolatase

Cited by 17 publications

References 14 publications

Urea transport-defective strains of Saccharomyces cerevisiae

Urea transport-defective strains of Saccharomyces cerevisiae

Induction of the Allantoin Degradative Enzymes in Saccharomyces cerevisiae by the Last Intermediate of the Pathway

Identification of the ureidoglycolate hydrolase gene in the DAL gene cluster of Saccharomyces cerevisiae.

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