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MetaCyc Pathway: glycolysis I (from glucose 6-phosphate)
Traceable author statement to experimental support

Pathway diagram: glycolysis I (from glucose 6-phosphate)

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Synonyms: Embden-Meyerhof pathway, Embden-Meyerhof-Parnas pathway, EMP pathway, glycolysis (plastidic)

Superclasses: Generation of Precursor Metabolites and EnergyGlycolysis

Some taxa known to possess this pathway include : Arabidopsis thaliana col, Brassica napus, Escherichia coli K-12 substr. MG1655, Mycoplasma pneumoniae M129, Ricinus communis, Saccharomyces cerevisiae, Spinacia oleracea, Zea mays

Expected Taxonomic Range: Archaea, Bacteria , Eukaryota

General Background

Glycolysis, which was first studied as a pathway for the utilization of glucose, is one of the major pathways of central metabolism, the other two being the pentose phosphate pathway and the TCA cycle. Glycolysis is essential under all conditions of growth, because it produces six of the 13 precursor metabolites that are the starting materials for the biosynthesis of building blocks for macromolecules and other needed small molecules (the six compounds are β-D-glucose 6-phosphate, β-D-fructofuranose 6-phosphate, glycerone phosphate, 3-phospho-D-glycerate, phosphoenolpyruvate, and pyruvate). Glycolysis can be found, if at least in part, in almost all organisms.

Even though glycolysis is often described starting with glucose, other hexoses (e.g. fructose) can also serve as input (as its name implies - glycose is a general term for simple sugars).

Glycolysis has evolved to fulfill two essential functions:

i) it oxidizes hexoses to generate ATP, reductants and pyruvate, and

ii) being an amphibolic pathway (pathway that involves both catabolism and anabolism), 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 and energy. 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 and phosphoenolpyruvate synthetase) that catalyze different irreversible reactions flowing in the opposite direction.

About This Pathway

This pathway diagram describes the well characterized glycolysis pathway of the bacterium Escherichia coli growing with β-D-glucopyranose as a source of carbon and energy. Glucose is not shown here as a component of glycolysis because when used by Escherichia coli , glucose enters the cell via a phosphotransferase system (transport of glucose, glucose PTS permease), and the first intracellular species, therefore, is β-D-glucose 6-phosphate.

Escherichia 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]. It may be required to supplement levels of glucose 6-phosphate under anabolic stress conditions [Arora95].

Other substrates may enter glycolysis at different stages. For example, the sugars and sugar alcohols D-allose, sorbose, D-mannitol, D-sorbitol, D-mannose and sucrose, which are processed into β-D-fructofuranose 6-phosphate, enter the pathway at that stage (see glycolysis II (from fructose 6-phosphate)).

For reviews, please see: Romeo, T. and J. L. Snoep, [ECOSAL] module 3.5.1.; Fraenkel, D. G. [Neidhardt96] p. 189-198.

Superpathways: superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass, superpathway of glycolysis and Entner-Doudoroff

Variants: glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis IV (plant cytosol), glycolysis V (Pyrococcus)

Unification Links: AraCyc:GLYCOLYSIS, EcoCyc:GLYCOLYSIS

Revised 26-Jan-2007 by Ingraham JL, UC Davis


Arora95: Arora KK, Pedersen PL (1995). "Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins." Arch Biochem Biophys 1995;319(2);574-8. PMID: 7786044

ECOSAL: EcoSal "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Meyer97: Meyer D, Schneider-Fresenius C, Horlacher R, Peist R, Boos W (1997). "Molecular characterization of glucokinase from Escherichia coli K-12." J Bacteriol 179(4);1298-306. PMID: 9023215

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.

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Abbe83: Abbe K, Takahashi S, Yamada T (1983). "Purification and properties of pyruvate kinase from Streptococcus sanguis and activator specificity of pyruvate kinase from oral streptococci." Infect Immun 39(3);1007-14. PMID: 6840832

Aguilera09: Aguilera L, Gimenez R, Badia J, Aguilar J, Baldoma L (2009). "NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase." Int Microbiol 12(3);187-92. PMID: 19784925

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

Alakent11: Alakent B, Baskan S, Doruker P (2011). "Effect of ligand binding on the intraminimum dynamics of proteins." J Comput Chem 32(3);483-96. PMID: 20730777

Albery76: Albery WJ, Knowles JR (1976). "Free-energy profile of the reaction catalyzed by triosephosphate isomerase." Biochemistry 15(25);5627-31. PMID: 999838

Albin84: Albin R, Silverman PM (1984). "Physical and genetic structure of the glpK-cpxA interval of the Escherichia coli K-12 chromosome." Mol Gen Genet 197(2);261-71. PMID: 6097795

Alefounder89: 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

Alefounder89a: 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

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

Anderson69: Anderson A, Cooper RA (1969). "Gluconeogenesis in Escherichia coli The role of triose phosphate isomerase." FEBS Lett 4(1);19-20. PMID: 11947134

Anderson75: Anderson L.E., Heinrikson R.L., Noyes C. "Chloroplast and cytoplasmic enzymes." Arch. Biochem. Biophys. (1975) 169:262-268.

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

Ashizawa91: Ashizawa K, McPhie P, Lin KH, Cheng SY (1991). "An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate." Biochemistry 30(29);7105-11. PMID: 1854723


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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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