Pyruvate Decarboxylase: An Indispensable Enzyme for Growth of Saccharomyces cerevisiae on Glucose

Flikweert, Marcel T.; ZANDEN, LINDA VAN DER; JANSSEN, WOUTER M. TH. M.; Steensma, H. Yde; Dijken, Johannes P. van; Pronk, Jack T.

doi:10.1002/(sici)1097-0061(19960315)12:3<247::aid-yea911>3.3.co;2-9

Cited by 190 publications

(153 citation statements)

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“…Enzyme Activities-The following cell extracts were broken using glass beads and assayed as described in the respective references: alcohol dehydrogenase and enolase (32), pyruvate decarboxylase (33), glyceraldehyde-3-phosphate dehydrogenase (34), catalase, and superoxide dismutase (SOD) (35). To determine Mn-SOD activity, 1 mM NaCN, which inhibits 95% of the CuZn-SOD activity, was added to the reaction mixture (36).…”

Section: Methodsmentioning

confidence: 99%

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Reverter-Branchat

Cabiscol

Tamarit

et al. 2004

Journal of Biological Chemistry

195

168

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Oxidative modifications of cellular components have been described as one of the main contributions to aged phenotype. In Saccharomyces cerevisiae, two distinct life spans can be considered, replicative and chronological. The relationship between both aging models is still not clear despite suggestions that these phenomena may be related. In this work, we show that replicative and chronological-aged yeast cells are affected by an oxidative stress situation demonstrated by increased protein carbonylation when compared with young cells. The data on the identification of these oxidatively modified proteins gives clues to better understand cellular dysfunction that occurs during aging. Strikingly, although in both aging models metabolic differences are important, major targets are almost the same. Common targets include stress resistance proteins (Hsp60 and Hsp70) and enzymes involved in glucose metabolism such as enolase, glyceraldehydes-3-P dehydrogenase, fructose-1,6-biphosphate aldolase, pyruvate decarboxylase, and alcohol dehydrogenase. In both aging models, calorie restriction results in decreased damage to these proteins. In addition, chronological-aged cells grown under glucose restriction displayed lowered levels of lipid peroxidation product lipofuscin. Intracellular iron concentration is kept almost unchanged, whereas in non-restricted cells, the values increase up 4 -5 times. The pro-oxidant effects of such increased iron concentration would account for the damage observed. Also, calorie-restricted cells show undamaged catalase, which clearly appears carbonylated in cells grown at a high glucose concentration. These results may explain lengthening of the viability of chronological-aged cells and could have an important role in replicative life span extension by calorie restriction.

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Section: Methodsmentioning

confidence: 99%

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Reverter-Branchat

Cabiscol

Tamarit

et al. 2004

Journal of Biological Chemistry

195

168

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“…Thus, the loss of ATP production through ethanolic fermentation is not the cause for the inhibition of tube growth on AEP. In Saccharomyces cerevisiae, triple pdc knockouts grow normally on ethanol but completely fail to grow on glucose (Flikweert et al, 1996). Because small amounts of C 2 compounds can rescue the defect, it was hypothesized that PDC has a biosynthetic function, providing cytosolic acetyl-CoA, in particular for lipid biosynthesis (van Maris et al, 2003).…”

Section: The In Vivo Function Of Pdc2 Is To Bypass Pdhmentioning

confidence: 99%

Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

et al. 2005

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Rapid pollen tube growth places unique demands on energy production and biosynthetic capacity. The aim of this work is to understand how primary metabolism meets the demands of such rapid growth. Aerobically grown pollen produce ethanol in large quantities. The ethanolic fermentation pathway consists of two committed enzymes: pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH). Because adh mutations do not affect male gametophyte function, the obvious question is why pollen synthesize an abundant enzyme if they could do just as well without. Using transposon tagging in Petunia hybrida, we isolated a null mutant in pollen-specific Pdc2. Growth of the mutant pollen tubes through the style is reduced, and the mutant allele shows reduced transmission through the male, when in competition with wild-type pollen. We propose that not ADH but rather PDC is the critical enzyme in a novel, pollen-specific pathway. This pathway serves to bypass pyruvate dehydrogenase enzymes and thereby maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction.

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“…6 Pdc activity was assayed as described elsewhere. 14 The protein concentration was determined using a Bradford reagent assay (Sigma) 15 with bovine serum albumin as a standard.…”

Section: Methodsmentioning

confidence: 99%

Production of pyruvate from mannitol by mannitol-assimilating pyruvate decarboxylase-negative Saccharomyces cerevisiae

et al. 2015

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Mannitol is contained in brown macroalgae up to 33% (w/w, dry weight), and thus is a promising carbon source for white biotechnology. However, Saccharomyces cerevisiae, a key cell factory, is generally regarded to be unable to assimilate mannitol for growth. We have recently succeeded in producing S. cerevisiae that can assimilate mannitol through spontaneous mutations of Tup1-Cyc8, each of which constitutes a general corepressor complex. In this study, we demonstrate production of pyruvate from mannitol using this mannitol-assimilating S. cerevisiae through deletions of all 3 pyruvate decarboxylase genes. The resultant mannitol-assimilating pyruvate decarboxylase-negative strain produced 0.86 g/L pyruvate without use of acetate after cultivation for 4 days, with an overall yield of 0.77 g of pyruvate per g of mannitol (the theoretical yield was 79%). Although acetate was not needed for growth of this strain in mannitol-containing medium, addition of acetate had a significant beneficial effect on production of pyruvate. This is the first report of production of a valuable compound (other than ethanol) from mannitol using S. cerevisiae, and is an initial platform from which the productivity of pyruvate from mannitol can be improved.

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Pyruvate Decarboxylase: An Indispensable Enzyme for Growth of Saccharomyces cerevisiae on Glucose

Cited by 190 publications

References 1 publication

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Pyruvate Decarboxylase Provides Growing Pollen Tubes with a Competitive Advantage in Petunia

Production of pyruvate from mannitol by mannitol-assimilating pyruvate decarboxylase-negative Saccharomyces cerevisiae

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