ArticleJournal of bacteriology2003
Glyceraldehyde-3-phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 68 citations in OpenAlex.
- Metabolic Engineering of Microorganisms to Produce Pyruvate and Derived Compounds.Molecules (Basel, Switzerland) · 2023Review
- Escherichia coli robustly expresses ATP synthase at growth rate-maximizing concentrations.The FEBS journal · 2022Article
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- Systems Biology - A Guide for Understanding and Developing Improved Strains of Lactic Acid Bacteria.Frontiers in microbiology · 2019Review
- Maintaining maximal metabolic flux by gene expression control.PLoS computational biology · 2018Article
- Adaptation of Lactococcus lactis to high growth temperature leads to a dramatic increase in acidification rate.Scientific reports · 2015Article
- How fast-growing bacteria robustly tune their ribosome concentration to approximate growth-rate maximization.The FEBS journal · 2015Article
- Engineering the glycolytic pathway: A potential approach for improvement of biocatalyst performance.Bioengineered · 2015Review
- Monte-Carlo modeling of the central carbon metabolism of Lactococcus lactis: insights into metabolic regulation.PloS one · 2014Article
- Repetitive, marker-free, site-specific integration as a novel tool for multiple chromosomal integration of DNA.Applied and environmental microbiology · 2013Article
- Optimality principles in the regulation of metabolic networks.Metabolites · 2012Article
- Overexpression of genes encoding glycolytic enzymes in Corynebacterium glutamicum enhances glucose metabolism and alanine production under oxygen deprivation conditions.Applied and environmental microbiology · 2012Article
- Assessing the contributions of the LiaS histidine kinase to the innate resistance of Listeria monocytogenes to nisin, cephalosporins, and disinfectants.Applied and environmental microbiology · 2012Article
- Systems biology of lactic acid bacteria: a critical review.Microbial cell factories · 2011Review
- GAP promoter library for fine-tuning of gene expression in Pichia pastoris.Applied and environmental microbiology · 2011Article
- Functional analysis of the role of CggR (central glycolytic gene regulator) in Lactobacillus plantarum by transcriptome analysis.Microbial biotechnology · 2011Article
- Key players in the genetic switch of bacteriophage TP901-1.Biophysical journal · 2011Article
- Properties and role of glyceraldehyde-3-phosphate dehydrogenase in the control of fermentation pattern and growth in a ruminal bacterium, Streptococcus bovis.Current microbiology · 2009Article
- Metabolic control analysis: a tool for designing strategies to manipulate metabolic pathways.Journal of biomedicine & biotechnology · 2008Review
- The las enzymes control pyruvate metabolism in Lactococcus lactis during growth on maltose.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has previously been suggested to have almost absolute control over the glycolytic flux in Lactococcus lactis (B. Poolman, B. Bosman, J. Kiers, and W. N. Konings, J. Bacteriol. 169:5887-5890, 1987). Those studies were based on inhibitor titrations with iodoacetate, which specifically inhibits GAPDH, and the data suggested that it should be possible to increase the glycolytic flux by overproducing GAPDH activity. To test this hypothesis, we constructed a series of mutants with GAPDH activities from 14 to 210% of that of the reference strain MG1363. We found that the glycolytic flux was unchanged in the mutants overproducing GAPDH. Also, a decrease in the GAPDH activity had very little effect on the growth rate and the glycolytic flux until 25% activity was reached. Below this activity level, the glycolytic flux decreased proportionally with decreasing GAPDH activity. These data show that GAPDH activity has no control over the glycolytic flux (flux control coefficient = 0.0) at the wild-type enzyme level and that the enzyme is present in excess capacity by a factor of 3 to 4. The early experiments by Poolman and coworkers were performed with cells resuspended in buffer, i.e., nongrowing cells, and we therefore analyzed the control by GAPDH under similar conditions. We found that the glycolytic flux in resting cells was even more insensitive to changes in the GAPDH activity; in this case GAPDH was also present in a large excess and had no control over the glycolytic flux.
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