Mitochondrial acetaldehyde dehydrogenase from Saccharomyces cerevisiae

Jacobson, Myron K.; Bernofsky, Carl

doi:10.1016/0005-2744(74)90502-6

Cited by 67 publications

(63 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Mitochondrial aldehyde dehydrogenase activity was not detected in glucose growing cells under any condition, which is in accordance with the low ALD4 and ALD5 mRNA levels under this condition (Figure 1) and glucose repression described in the literature (Jacobson and Bernofsky, 1974). However, post-transcriptional mechanisms should also be considered, taking into account that transcripts corresponding to these two genes are detected under these conditions.…”

Section: Aldehyde Dehydrogenase Activity Is Higher In Ethanol Growingsupporting

confidence: 90%

“…The major cytosolic enzyme uses NADP + as co-enzyme, is activated by Mg 2+ and is not glucose-repressed (Dickinson, 1996;Meaden et al, 1997). The major mitochondrial enzyme uses NAD + and NADP + as co-enzymes, it is activated by K + and thiols and its expression is highly glucose-repressed (Jacobson and Bernofsky, 1974). Traditionally, cytosolic enzymes have been considered responsible for the formation of acetate from glucose while the main role of mitochondrial enzymes would take place during growth on ethanol (Wang et al, 1998;Saigal et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain‐dependent regulation of several ALD genes and is mediatedby the general stress response pathway

Aranda¹,

Olmo²

2003

Yeast

View full text Add to dashboard Cite

One of the stress conditions that yeast may encounter is the presence of acetaldehyde. In a previous study we identified that, in response to this stress, several HSP genes are induced that are also involved in the response to other forms of stress. Aldehyde dehydrogenases (ALDH) play an important role in yeast acetaldehyde metabolism (e.g. when cells are growing in ethanol). In this work we analyse the expression of the genes encoding these enzymes (ALD) and also the corresponding enzymatic activities under several growth conditions. We investigate three kinds of yeast strains: laboratory strains, strains involved in the alcoholic fermentation stage of wine production and flor yeasts (responsible for the biological ageing of sherry wines). The latter are very important to consider because they grow in media containing high ethanol concentrations, and produce important amounts of acetaldehyde. Under several growth conditions, further addition of acetaldehyde or ethanol in flor yeasts induced the expression of some ALD genes and led to an increase in ALDH activity. This result is consistent with their need to obtain energy from ethanol during biological ageing processes. Our data also suggest that post-transcriptional and/or post-translational mechanisms are involved in regulating the activity of these enzymes. Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.

show abstract

Section: Aldehyde Dehydrogenase Activity Is Higher In Ethanol Growingsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain‐dependent regulation of several ALD genes and is mediatedby the general stress response pathway

Aranda¹,

Olmo²

2003

Yeast

View full text Add to dashboard Cite

show abstract

“…Similar calculations for growth on ethanol are complicated by the fact that in yeasts several isoenzymes may occur of the first two enzymes involved in the metabolism of ethanol, alcohol dehydroge- nases and acetaldehyde dehydrogenases. Alcohol dehydrogenases are found in the cytosol (at least two forms) and in the mitochondria (Branden et al 1975;Fraenkel 1982).Acetaldehyde dehydrogenases are also found in both mitochondria and cytosol (Jacobson & Bernofsky 1974;Llorente & Ntifiez de Castro 1977). Indeed, even mitochondria isolated from glucose-limited chemostat cultures of S. cerevisiae grown at a low dilution rate oxidize both ethanol and acetaldehyde (van Urk et al 1989).…”

Section: Compartmentation and P/o-ratiomentioning

confidence: 99%

A theoretical evaluation of growth yields of yeasts

Verduyn

Stouthamer

Scheffers

et al. 1991

Antonie van Leeuwenhoek

212

176

View full text Add to dashboard Cite

Growth yields of Saccharomyces cerevisiae and Candida utilis in carbon-limited chemostat cultures were evaluated. The yields on ethanol and acetate were much lower in S. cerevisiae, in line with earlier reports that site I phosphorylation is absent in this yeast. However, during aerobic growth on glucose both organisms had the same cell yield. This can be attributed to two factors: -S. cerevisiae had a lower protein content than C. utilis; -uptake of glucose by C. utilis requires energy whereas in S. cerevisiae it occurs via facilitated diffusion. Theoretical calculations showed that, as a result of these two factors, the ATP requirement for biomass formation in C. utilis is 35% higher than in S. cerevisiae (theoretical YATP values of 20.8 and 28.1, respectively). The experimental YATP for anaerobic growth of S. cerevisiae on glucose was 16 g biomass-mol ATP -1.In vivo P/O-ratios can be calculated for aerobic growth on ethanol and acetate, provided that the gap between the theoretical and experimental ATP requirements as observed for growth on glucose is taken into account. This was done in two ways: -via the assumption that the gap is independent of the growth substrate (i.e. a fixed amount of ATP bridges the difference between the theoretical and experimental values). -alternatively, on the assumption that the difference is a fraction of the total ATP expenditure, that is dependent on the substrate. Calculations of P/O-ratios for growth of both yeasts on glucose, ethanol, and acetate made clear that only by assuming a fixed difference between theoretical and experimental ATP requirements, the P/O-ratios are more or less independent of the growth substrate. These P/O-ratios are approximately 30% lower than the calculated mechanistic values.

show abstract

“…The first step in this bypass is the decarboxylation of pyruvate to acetaldehyde catalysed by cytosolic pyruvate decarboxylase (Barnett, 1976). Subsequently, acetaldehyde is converted to acetate by acetaldehyde dehydrogenase (Jacobson and Bernofsky, 1974) and acetate is converted to CoASAc by acetyl-coenzyme A synthetase Table 1. Saccharomyces cerevisiae strains.…”

mentioning

confidence: 99%

Regulation of the PDA1 gene encoding the E1α subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae

Wenzel

Luttik

Berg

et al. 1993

European Journal of Biochemistry

View full text Add to dashboard Cite

Expression of the PDAl gene encoding the E l a subunit of the pyruvate dehydrogenase complex (PDH complex) and activity of the complex were investigated in cells grown under several conditions. Comparable amounts of PDAl mRNA and E l a subunit were detected in cells from batch and chemostat cultures grown on various carbon sources, showing constitutive expression of P DAl at the transcriptional and translational levels. Induction of the regulatory GCN4 mechanism upon histidine starvation, using the anti-metabolite 3-amino-l,2,4-triazole, increased the levels of PDAl mRNA by approximately 40%. However, a corresponding increase of E l a concentration or activity of the PDH complex could not be detected. Hence, expression of the PDAI gene is only regulated to a small extent, if at all, by the GCN4 mechanism.Contrary to the constant levels of PDAl mRNA and Ela subunit in both batch and chemostat cultures, the specific activity of the PDH complex varied with the culture conditions. The activity of the PDH complex in chemostat cultures was approximately two-threefold higher than in batch cultures grown on the same carbon sources. Overproduction of the E l a subunit in batch cultures resulted in a two-threefold increase in the activity of the PDH complex. Taken together, these results indicate that the activity of the PDH complex is mainly regulated by post-translational modification of the E l a subunit.Expression of PDAl and activity of the PDH complex were also detected in cultures grown under conditions where no physiological significance of the PDH complex was expected, i.e. during anaerobic growth on glucose or aerobic growth on ethanol. Apparently, the switch from oxidative growth to fermentation occurs without much effect on the PDH complex. These observations suggest that the PDH complex has an alternative function besides sugar catabolism.

show abstract

Mitochondrial acetaldehyde dehydrogenase from Saccharomyces cerevisiae

Cited by 67 publications

References 32 publications

Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain‐dependent regulation of several ALD genes and is mediatedby the general stress response pathway

Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain‐dependent regulation of several ALD genes and is mediatedby the general stress response pathway

A theoretical evaluation of growth yields of yeasts

Regulation of the PDA1 gene encoding the E1α subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae

Contact Info

Product

Resources

About