Degradation of organic nitrogen compounds by yeasts

Large, Peter J.

doi:10.1002/yea.320020102

Cited by 118 publications

(100 citation statements)

References 169 publications

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“…Expression of SPAO1 allows S. cerevisiae cells to utilize ethylamine as a nitrogen source, except in copper-starved atx1D and ccc2D null mutants S. cerevisiae cells lack the ability to utilize primary amines such as ethylamine as a nitrogen source to support their growth (Large, 1986), an observation that was recapitulated in the present study. As shown in Fig.…”

Section: Spao1supporting

confidence: 67%

“…pombe Genome Project revealed two putative ORFs, SPAC2E1P3.04 and SPBC1289.16c, encoding proteins related to the CAO family of enzymes (Jalkanen & Salmi, 2001 ) that may promote the active conformation of TPQ during the enzymic reaction. To ascertain the potential role of spao1 + and spao2 + in nitrogen and carbon metabolism, we expressed these genes in S. cerevisiae, an organism that does not possess endogenous CAOs (Large, 1986), thereby providing an excellent background for their characterization. The spao1 + and spao2 + genes were placed under the control of the ADH or GPD gene promoter.…”

Section: Resultsmentioning

confidence: 99%

“…Curiously, S. cerevisiae is one of the few yeast species that does not have an endogenous CAO (Cai & Klinman, 1994b;Large, 1986). However, heterologous expression of a CAO from another organism in S. cerevisiae produces a functional enzyme (Cai & Klinman, 1994a).…”

Section: Introductionmentioning

confidence: 99%

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Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae

Laliberté

Labbé

2006

Microbiology

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Copper amine oxidases (CAOs) are found in almost every living kingdom. Although Saccharomyces cerevisiae is one of the few yeast species that lacks an endogenous CAO, heterologous gene expression of CAOs from other organisms produces a functional enzyme. To begin to characterize their function and mechanisms of copper acquisition, two putative cao + genes from Schizosaccharomyces pombe were expressed in S. cerevisiae. Expression of spao1 + resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. On the other hand, expression of spao2 + failed to produce an active CAO. Using a functional spao1 + -GFP fusion allele, the SPAO1 protein was localized in the cytosol. Under copper-limiting conditions, yeast cells harbouring deletions of the MAC1, CTR1 and CTR3 genes were defective in amine oxidase activity. Likewise, atx1D null cells exhibited no CAO activity, while ccc2D mutant cells exhibited decreased levels of amine oxidase activity, and mutations in cox17D and ccs1D did not cause any defects in this activity. Copper-deprived S. cerevisiae cells expressing spao1 + required a functional atx1 + gene for growth on minimal medium containing ethylamine as the sole nitrogen source. Under these conditions, the inability of the atx1D cells to utilize ethylamine correlated with the lack of SPAO1 activity, in spite of the efficient expression of the protein. Cells carrying a disrupted ccc2D allele exhibited only weak growth on ethylamine medium containing a copper chelator. The results of these studies reveal that expression of the heterologous spao1 + gene in S. cerevisiae is required for its growth in medium containing ethylamine as the sole nitrogen source, and that expression of an active Schiz. pombe SPAO1 protein in S. cerevisiae depends on the acquisition of copper through the high-affinity copper transporters Ctr1 and Ctr3, and the copper chaperone Atx1.

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Section: Spao1supporting

confidence: 67%

Section: Resultsmentioning

confidence: 99%

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Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae

Laliberté

Labbé

2006

Microbiology

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“…During fermentation amino acids, free and in peptide form, are taken up from the medium by the cell. Free amino acids are incorporated directly without modification into proteins, or degraded by the cell and the nitrogen is used for the synthesis of other nitrogenous cell constituents and the amino acid derivative keto-acids may be used by the cell for synthetic purposes 16 . The assimilation of wort amino acids is ordered and groups of amino acids have been identified on the basis of the rate of removal from the fermentation broth 26 .…”

Section: Discussionmentioning

confidence: 99%

Effect of Sugar Catabolite Repression in Correlation with the Structural Complexity of the Nitrogen Source on Yeast Growth and Fermentation

Cruz

Batistote

Ernandes

2003

Journal of the Institute of Brewing

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Biomass and ethanol production by industrial Saccharomyces cerevisiae strains were strongly affected by the structural complexity of the nitrogen source during fermentation in media containing galactose, and supplemented with a nitrogen source varying from a single ammonium salt (ammonium sulfate) to free amino acids (casamino acids) and peptides (peptone). Diauxie was observed at low galactose concentrations independent of nitrogen supplementation. At high sugar concentrations altered patterns of galactose utilisation were observed. Biomass accumulation and ethanol production depended on the nature of the nitrogen source and were different for baking and brewing ale and lager strains. Baking yeast showed improved galactose fermentation performance in the medium supplemented with casamino acids. High biomass production was observed with peptone and casamino acids for the ale brewing strain, however high ethanol production was observed only in the presence of casamino acids. Conversely, peptone was the nitrogen supplement that induced higher biomass and ethanol production for the lager brewing strain. Ammonium salts always induced poor yeast performance. The results with galactose differed from those obtained with glucose and maltose which indicated that supplementation with a nitrogen source in the peptide form (peptone) was more positive for yeast metabolism, suggesting that sugar catabolite repression has a central role in yeast performance in a medium containing nitrogen sources with differing levels of structural complexity.

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“…We investigated the kinetics of the GOGAT and NADP+-dependent GDH activities in extracts of batch-culture cells. NAD+-dependent GDH has a catabolic function in yeasts (Large, 1986) and therefore was not subjected to kinetic analysis in this study. GS kinetics was not examined in detail as initial experiments revealed that maximal velocity, V , was obtained at < 20 pM-ammonium.…”

mentioning

confidence: 99%

Ammonium Assimilation by Candida albicans and Other Yeasts: Evidence for Activity of Glutamate Synthase

et al. 1989

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Activities and properties of the ammonium assimilation enzymes NADP+-dependent glutamate dehydrogenase (GDH), glutamate synthase (GOGAT) and glutamine synthetase (GS) were determined in batch and continuous cultures of Candida albicans. NADP+-dependent GDH activity showed allosteric kinetics, with an So.s for 2-oxoglutarate of 7.5 mM and an apparent K , for ammonium of 5-0 mM. GOGAT activity was affected by the buffer used for extraction and assay, but in phosphate buffer, kinetics were hyperbolic, yielding K , values for glutamine of 750 p~ and for 2-oxoglutarate of 65 p~. The enzymes GOGAT and NADP+-dependent GDH were also assayed in batch cultures of Saccharomyces cerevisiae and three other pathogenic Candida spp. : Candida tropicalis, Candida pseudotropicalis and Candida parapsilosis. Evidence is presented that GSlGOGAT is a major pathway for ammonium assimilation in Candida albicans and that this pathway is also significant in other Candida species.

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Degradation of organic nitrogen compounds by yeasts

Cited by 118 publications

References 169 publications

Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae

Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae

Effect of Sugar Catabolite Repression in Correlation with the Structural Complexity of the Nitrogen Source on Yeast Growth and Fermentation

Ammonium Assimilation by Candida albicans and Other Yeasts: Evidence for Activity of Glutamate Synthase

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