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Pathway Description
Glycolysis
Escherichia coli K-12
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2024-09-10
Last Updated: 2025-05-08
Glycolysis is a metabolic pathway consisting of ten reactions that convert glucose to pyruvate, releasing energy to form ATP and NADH. It occurs in two phases: the chemical priming phase and the energy-yielding phase. In the priming phase, D-glucose, which can be imported or derived from galactose metabolism, is phosphorylated to glucose-6-phosphate by a hexokinase-like enzyme, using ATP. This is then converted to fructose-6-phosphate, which is further phosphorylated to fructose-1,6-bisphosphate by 6-phosphofructokinase, also using ATP. Aldolase then splits fructose-1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde-3-phosphate, which can interconvert via triosephosphate isomerase. In the energy-yielding phase, glyceraldehyde-3-phosphate is converted to 1,3-bisphosphoglycerate by glyceraldehyde-3-phosphate dehydrogenase, producing NADH in the process. ATP is generated when 1,3-bisphosphoglycerate is converted to 3-phosphoglycerate. Further steps involve the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase, followed by conversion to phosphoenolpyruvate by enolase. Finally, pyruvate kinase converts phosphoenolpyruvate to pyruvate, producing ATP in the process. Pyruvate then participates in further metabolic pathways, including pyruvate metabolism, tyrosine metabolism, and the synthesis of pantothenate and CoA.
References
Glycolysis References
Kanehisa, M., 2002, November. The KEGG database. In ‘In silico’simulation of biological processes: Novartis Foundation Symposium 247 (Vol. 247, pp. 91-103). Chichester, UK: John Wiley & Sons, Ltd.
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Berg, J.M., Tymoczko, J.L., Stryer, L. Biochemistry (5th ed) (2002). W. H. Freeman, New York.
Erni B, Zanolari B: Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc. J Biol Chem. 1986 Dec 15;261(35):16398-403.
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Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. doi: 10.1093/dnares/3.3.137.
Pubmed: 8905232
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Pubmed: 9278503
De Reuse H, Danchin A: The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription. J Bacteriol. 1988 Sep;170(9):3827-37. doi: 10.1128/jb.170.9.3827-3837.1988.
Pubmed: 2457575
Saffen DW, Presper KA, Doering TL, Roseman S: Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes. J Biol Chem. 1987 Nov 25;262(33):16241-53.
Pubmed: 2960675
Yang Y, Zhao G, Winkler ME: Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia coli K-12. FEMS Microbiol Lett. 1996 Jul 15;141(1):89-95. doi: 10.1111/j.1574-6968.1996.tb08368.x.
Pubmed: 8764513
Kabir MM, Shimizu K: Gene expression patterns for metabolic pathway in pgi knockout Escherichia coli with and without phb genes based on RT-PCR. J Biotechnol. 2003 Oct 9;105(1-2):11-31.
Pubmed: 14511906
Froman BE, Tait RC, Gottlieb LD: Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli. Mol Gen Genet. 1989 May;217(1):126-31. doi: 10.1007/bf00330951.
Pubmed: 2549364
Smith MW, Doolittle RF: Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase. J Mol Evol. 1992 Jun;34(6):544-5.
Pubmed: 1593646
Daldal F: Nucleotide sequence of gene pfkB encoding the minor phosphofructokinase of Escherichia coli K-12. Gene. 1984 Jun;28(3):337-42. doi: 10.1016/0378-1119(84)90151-3.
Pubmed: 6235149
Daldal F: Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme. J Mol Biol. 1983 Aug 5;168(2):285-305. doi: 10.1016/s0022-2836(83)80019-9.
Pubmed: 6310120
Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Thomson GJ, Howlett GJ, Ashcroft AE, Berry A: The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase. Biochem J. 1998 Apr 15;331 ( Pt 2):437-45. doi: 10.1042/bj3310437.
Pubmed: 9531482
Nelson K, Whittam TS, Selander RK: Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6667-71. doi: 10.1073/pnas.88.15.6667.
Pubmed: 1862091
Branlant G, Branlant C: Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem. 1985 Jul 1;150(1):61-6. doi: 10.1111/j.1432-1033.1985.tb08988.x.
Pubmed: 2990926
Alefounder PR, Perham RN: 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. 1989 Jun;3(6):723-32. doi: 10.1111/j.1365-2958.1989.tb00221.x.
Pubmed: 2546007
Spring TG, Wold F: The purification and characterization of Escherichia coli enolase. J Biol Chem. 1971 Nov 25;246(22):6797-802.
Pubmed: 4942326
Dannelly HK, Duclos B, Cozzone AJ, Reeves HC: Phosphorylation of Escherichia coli enolase. Biochimie. 1989 Sep-Oct;71(9-10):1095-100. doi: 10.1016/0300-9084(89)90116-8.
Pubmed: 2513001
Chandran V, Luisi BF: Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol. 2006 Apr 21;358(1):8-15. doi: 10.1016/j.jmb.2006.02.012. Epub 2006 Feb 21.
Pubmed: 16516921
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0290558
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