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Pathway Description
Glycolysis and Pyruvate Dehydrogenase
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-03-01
Last Updated: 2019-08-13
Fructose metabolism begins with the transport of beta-D-glucose 6-phosphate through a glucose PTS permease. This compound is isomerized by a glucose-6-phosphate isomerase resulting in fructose 6-phosphate. This compound can be phosphorylated by two different enzymes: a pyridoxal phosphatase/fructose 1,6-bisphosphatase or an ATP-driven 6-phosphofructokinase-1, resulting in fructose 1,6-biphosphate. This compound can either react with a fructose bisphosphate aldolase class 1 resulting in D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate or through a fructose biphosphate aldolase class 2 resulting in D-glyceraldehyde 3-phosphate. This compound can then either react in a reversible triosephosphate isomerase resulting in dihydroxyacetone phosphate or react with a phosphate through an NAD-dependent glyceraldehyde 3-phosphate dehydrogenase resulting in glyceric acid 1,3-biphosphate. This compound is dephosphorylated by a phosphoglycerate kinase resulting in 3-phosphoglyceric acid. This compound, in turn, can either react with a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase or a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase resulting in 2-phospho-D-glyceric acid. This compound interacts with an enolase resulting in a phosphoenolpyruvic acid and water. Phosphoenolpyruvic acid can react either through an AMP-driven phosphoenoylpyruvate synthase or an ADP-driven pyruvate kinase protein complex resulting in pyruvic acid. The pyruvic acid reacts with CoA through an NAD-driven pyruvate dehydrogenase complex resulting in carbon dioxide and an acetyl-CoA which gets incorporated into the TCA cycle pathway.
References
Glycolysis and Pyruvate Dehydrogenase References
Hollinshead WD, Rodriguez S, Martin HG, Wang G, Baidoo EE, Sale KL, Keasling JD, Mukhopadhyay A, Tang YJ: Examining Escherichia coli glycolytic pathways, catabolite repression, and metabolite channeling using Deltapfk mutants. Biotechnol Biofuels. 2016 Oct 10;9:212. doi: 10.1186/s13068-016-0630-y. eCollection 2016.
Pubmed: 27766116
Escherichia coli and Salmonella: Cellular and Molecular Biology (EcoSal). Online edition.
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
Donahue JL, Bownas JL, Niehaus WG, Larson TJ: Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J Bacteriol. 2000 Oct;182(19):5624-7. doi: 10.1128/jb.182.19.5624-5627.2000.
Pubmed: 10986273
Truniger V, Boos W, Sweet G: Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri. J Bacteriol. 1992 Nov;174(21):6981-91. doi: 10.1128/jb.174.21.6981-6991.1992.
Pubmed: 1400248
Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. doi: 10.1093/nar/21.15.3391.
Pubmed: 8346018
Sedivy JM, Daldal F, Fraenkel DG: Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion. J Bacteriol. 1984 Jun;158(3):1048-53.
Pubmed: 6327623
Hamilton WD, Harrison DA, Dyer TA: Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene. Nucleic Acids Res. 1988 Sep 12;16(17):8707. doi: 10.1093/nar/16.17.8707.
Pubmed: 2843822
Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. doi: 10.1093/nar/23.12.2105.
Pubmed: 7610040
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
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
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
Maupin-Furlow JA, Rosentel JK, Lee JH, Deppenmeier U, Gunsalus RP, Shanmugam KT: Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli. J Bacteriol. 1995 Sep;177(17):4851-6. doi: 10.1128/jb.177.17.4851-4856.1995.
Pubmed: 7665460
Walkenhorst HM, Hemschemeier SK, Eichenlaub R: Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene. Microbiol Res. 1995 Nov;150(4):347-61. doi: 10.1016/S0944-5013(11)80016-9.
Pubmed: 8564363
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
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
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
Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. doi: 10.1093/nar/22.13.2576.
Pubmed: 8041620
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