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 Energy → Glycolysis|
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
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:
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)).
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.
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
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
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
Showing only 20 references. To show more, press the button "Show all references".
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493