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4 - Glycolysis

Published online by Cambridge University Press:  05 September 2012

Byung Hong Kim  and
Geoffrey Michael Gadd
Byung Hong Kim
Affiliation:
Korea Institute of Science and Technology, Seoul
Geoffrey Michael Gadd
Affiliation:
University of Dundee
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Summary

Escherichia coli can grow on a simple medium containing glucose and mineral salts and this bacterium can synthesize all cell constituents using materials provided in this medium. Glucose is metabolized through the Embden–Meyerhof–Parnas (EMP) pathway and hexose monophosphate (HMP) pathway and the metabolic product, pyruvate, is decarboxylated oxidatively to acetyl-CoA to be oxidized through the tricarboxylic acid (TCA) cycle. Twelve intermediates of these pathways are used as carbon skeletons for biosynthesis (Table 4.1). Heterotrophs that utilize organic compounds other than carbohydrates convert their substrates into one or more of these intermediates. For this reason, glucose metabolism through glycolysis and the TCA cycle is called central metabolism.

Eukaryotes metabolize glucose through the EMP pathway to generate ATP, pyruvate and NADH, and the HMP pathway is needed to supply the metabolic intermediates not available from the EMP pathway such as pentose-5-phosphate and erythrose-4-phosphate, and NADPH. Most prokaryotes employ similar mechanisms, but some prokaryotes metabolize glucose through unique pathways known only in prokaryotes, e.g. the Entner–Doudoroff (ED) pathway and phosphoketolase (PK) pathway. Some prokaryotes have genes for the ED pathway in addition to the EMP pathway: genes for these pathways are expressed at the same time in several prokaryotes including a thermophilic bacterium (Thermotoga maritima), a thermophilic archaeon (Thermoproteus tenax) and a halophilic archaeon (Halococcus saccharolyticus). Escherichia coli metabolizes glucose via the EMP pathway, but gluconate is oxidized through the ED pathway. Modified EMP and ED pathways are quite common in archaea.

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Bacterial Physiology and Metabolism , pp. 60 - 84
Publisher: Cambridge University Press
Print publication year: 2008

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References

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Liyanage, H., Kashket, S., Young, M. & Kashket, E. R. (2001). Clostridium beijerinckii and Clostridium difficile detoxify methylglyoxal by a novel mechanism involving glycerol dehydrogenase. Applied and Environmental Microbiology 67, 2004–2010.CrossRefGoogle ScholarPubMed
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Xu, D., Liu, X., Guo, C. & Zhao, J. (2006). Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002. Microbiology-UK 152, 2013–2021.CrossRefGoogle ScholarPubMed
Alves, A. M. C. R., Euverink, G. J. W., Santos, H. & Dijkhuizen, L. (2001). Different physiological roles of ATP- and PPi-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica. Journal of Bacteriology 183, 7231–7240.CrossRefGoogle Scholar
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Grochowski, L. L., Xu, H. & White, R. H. (2005). Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii occurs in the absence of a pentose-phosphate pathway. Journal of Bacteriology 187, 7382–7389.CrossRefGoogle ScholarPubMed
Pernestig, A. K., Georgellis, D., Romeo, T., Suzuki, K., Tomenius, H., Normark, S. & Melefors, O. (2003). The Escherichia coli BarA-UvrY two-component system is needed for efficient switching between glycolytic and gluconeogenic carbon sources. Journal of Bacteriology 185, 843–853.CrossRefGoogle ScholarPubMed
Tjaden, B., Plagens, A., Dorr, C., Siebers, B. & Hensel, R. (2006). Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase of Thermoproteus tenax: key pieces in the puzzle of archaeal carbohydrate metabolism. Molecular Microbiology 60, 287–298.CrossRefGoogle ScholarPubMed
Verhees, C. H., Akerboom, J., Schiltz, E., Vos, W. M. & Oost, J. (2002). Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus. Journal of Bacteriology 184, 3401–3405.CrossRefGoogle ScholarPubMed
Wolfe, A. J. (2005). The acetate switch. Microbiology and Molecular Biology Reviews 69, 12–50.CrossRefGoogle ScholarPubMed
Christensen, J., Christiansen, T., Gombert, A. K., Thykaer, J. & Nielsen, J. (2001). Simple and robust method for estimation of the split between the oxidative pentose phosphate pathway and the Embden-Meyerhof-Parnas pathway in microorganisms. Biotechnology and Bioengineering 74, 517–523.CrossRefGoogle ScholarPubMed
Gibson, J. L. & Tabita, F. R. (1996). The molecular regulation of the reductive pentose phosphate pathway in proteobacteria and cyanobacteria. Archives in Microbiology 166, 141–150.CrossRefGoogle ScholarPubMed
Orita, I., Sato, T., Yurimoto, H., Kato, N., Atomi, H., Imanaka, T. & Sakai, Y. (2006). The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis. Journal of Bacteriology 188, 4698–4704.CrossRefGoogle ScholarPubMed
Takayama, S., McGarvey, G. J. & Wong, C. H. (1997). Microbial aldolases and transketolases: new biocatalytic approaches to simple and complex sugars. Annual Review of Microbiology 51, 285–310.CrossRefGoogle ScholarPubMed
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  • Glycolysis
  • Byung Hong Kim, Korea Institute of Science and Technology, Seoul, Geoffrey Michael Gadd, University of Dundee
  • Book: Bacterial Physiology and Metabolism
  • Online publication: 05 September 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511790461.005
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  • Glycolysis
  • Byung Hong Kim, Korea Institute of Science and Technology, Seoul, Geoffrey Michael Gadd, University of Dundee
  • Book: Bacterial Physiology and Metabolism
  • Online publication: 05 September 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511790461.005
Available formats
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  • Glycolysis
  • Byung Hong Kim, Korea Institute of Science and Technology, Seoul, Geoffrey Michael Gadd, University of Dundee
  • Book: Bacterial Physiology and Metabolism
  • Online publication: 05 September 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511790461.005
Available formats
×