If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: Embden-Meyerhof pathway, glucose degradation, Embden-Meyerhof-Parnas pathway, EMP pathway, glycolysis (plastidic), glycolysis I
|Superclasses:||Generation of Precursor Metabolites and Energy → Glycolysis|
Glycolysis, which was first studied as a pathway for the utilization of glucose, is one of the components of central metabolism, the other two being the pentose phosphate pathway and the TCA cycle I (prokaryotic). As such, its functioning is essential under all conditions of growth because it produces six (β-D-glucose 6-phosphate, β-D-fructofuranose 6-phosphate, dihydroxyacetone phosphate, 3-phospho-D-glycerate, phosphoenolpyruvate, and pyruvate) of the 13 precursor metabolites that are the starting materials for the biosynthesis of building blocks for macromolecules and other needed small molecules. Glycolysis can be found, if at least in part, in all organisms.
Glycolysis has evolved as a catabolic anaerobic pathway that fulfills two essential functions:
ii) it is an amphibolic pathway (pathway that involves both catabolism and anabolism) because it can reversibly produce hexoses from various low-molecular weight molecules.
Because various degradation pathways feed into glycolysis at many different points, glycolysis or portions of it run in the forward or reverse direction, depending on the carbon source being utilized, in order to satisfy the cell's need for precursor metabolites. This switching of direction is possible because all but two of the enzymatic reactions comprising glycolysis are reversible, and the conversions catalyzed by the two exceptions are rendered functionally reversible by other enzymes (fructose-1,6-bisphosphatase I and phosphoenolpyruvate synthetase) that catalyze different irreversible reactions flowing in the opposite direction.
About This Pathway
Glucose is not shown here as a component of glycolysis because when used by E. coli as a source of carbon and energy, glucose enters the cell via a phosphotransferase system (transport of glucose, glucose PTS permease), the first intracellular species, therefore, being glucose-6-phosphate. E. coli does constitutively produce glucokinase (the intracellular enzyme that converts glucose to glucose-6-phosphate) but it is not needed for the utilization of either exogenous or endogenous glucose [Meyer97]. Under anabolic stress conditions, it may be required to supplement levels of glucose 6-phosphate [Arora95].
For reviews, please see:
Romeo, T. and J. L. Snoep, [ECOSAL] module 3.5.1.
Fraenkel, D. G. Glycolysis. Escherichia coli and Salmonella, 2nd edition, Vol I, 189-198. [Neidhardt96]
Variants: glycolysis II (from fructose-6P)
Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.
Ahn11: Ahn J, Chung BK, Lee DY, Park M, Karimi IA, Jung JK, Lee H (2011). "NADPH-dependent pgi-gene knockout Escherichia coli metabolism producing shikimate on different carbon sources." FEMS Microbiol Lett 324(1);10-6. PMID: 22092758
AitBara10: Ait-Bara S, Carpousis AJ (2010). "Characterization of the RNA degradosome of Pseudoalteromonas haloplanktis: conservation of the RNase E-RhlB interaction in the gammaproteobacteria." J Bacteriol 192(20);5413-23. PMID: 20729366
Al04: Al Zaid Siddiquee K, Arauzo-Bravo MJ, Shimizu K (2004). "Metabolic flux analysis of pykF gene knockout Escherichia coli based on 13C-labeling experiments together with measurements of enzyme activities and intracellular metabolite concentrations." Appl Microbiol Biotechnol 63(4);407-17. PMID: 12802531
Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554
Alefounder89: Alefounder PR, Baldwin SA, Perham RN, Short NJ (1989). "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Biochem J 1989;257(2);529-34. PMID: 2649077
Alefounder89a: Alefounder PR, Perham RN (1989). "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Mol Microbiol 3(6);723-32. PMID: 2546007
Alvarez98: Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D (1998). "Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties." J Biol Chem 273(4);2199-206. PMID: 9442062
Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699
Auzat92: Auzat I, Garel JR (1992). "pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli: implications for the role of Asp 127." Protein Sci 1(2);254-8. PMID: 1304907
Auzat94: Auzat I, Le Bras G, Garel JR (1994). "The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP." Proc Natl Acad Sci U S A 91(12);5242-6. PMID: 8202475
Auzat94a: Auzat I, Le Bras G, Branny P, De La Torre F, Theunissen B, Garel JR (1994). "The role of Glu187 in the regulation of phosphofructokinase by phosphoenolpyruvate." J Mol Biol 235(1);68-72. PMID: 7904653
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