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Escherichia coli K-12 substr. MG1655 Pathway: sedoheptulose bisphosphate bypass
Inferred from experiment

Pathway diagram: sedoheptulose bisphosphate bypass

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

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic

Genetic regulation schematic for sedoheptulose bisphosphate bypass

Superclasses: Generation of Precursor Metabolites and Energy

Accumulation of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway (non-oxidative branch), leads to its utilization via the sedoheptulose bisphospate bypass pathway, described here. The pathway was discovered due to the unexpected near-wild type growth of a talA talB double null mutant on xylose [Nakahigashi09].

6-Phosphofructokinase I is able to phosphorylate D-sedoheptulose 7-phosphate, producing D-sedoheptulose-1,7-bisphosphate, which is in turn split into glycerone phosphate and D-erythrose 4-phosphate by fructose bisphosphate aldolase.

Created 23-Sep-2010 by Keseler I, SRI International


Nakahigashi09: Nakahigashi K, Toya Y, Ishii N, Soga T, Hasegawa M, Watanabe H, Takai Y, Honma M, Mori H, Tomita M (2009). "Systematic phenome analysis of Escherichia coli multiple-knockout mutants reveals hidden reactions in central carbon metabolism." Mol Syst Biol 5;306. PMID: 19756045

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

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

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

Auzat95: Auzat I, Byrnes WM, Garel JR, Chang SH (1995). "Role of residue 161 in the allosteric transitions of two bacterial phosphofructokinases." Biochemistry 34(21);7062-8. PMID: 7766616

Auzat95a: Auzat I, Le Bras G, Garel JR (1995). "Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli." J Mol Biol 246(2);248-53. PMID: 7869376

Auzat95b: Auzat I, Gawlita E, Garel JR (1995). "Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli." J Mol Biol 249(2);478-92. PMID: 7783204

Auzat97: Auzat I, Le Bras G, Garel JR (1997). "Allosteric activation increases the maximum velocity of E. coli phosphofructokinase." J Mol Biol 267(3);476-80. PMID: 9126831

Babul88: Babul J, Fraenkel DG (1988). "Phosphate modification of fructose-1,6-bisphosphate aldolase in Escherichia coli." Biochem Biophys Res Commun 151(3);1033-8. PMID: 3281666

Babul93: Babul J, Clifton D, Kretschmer M, Fraenkel DG (1993). "Glucose metabolism in Escherichia coli and the effect of increased amount of aldolase." Biochemistry 32(17);4685-92. PMID: 8485146

Baldwin78: Baldwin SA, Perham RN (1978). "Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);643-52. PMID: 348198

Baldwin78a: Baldwin SA, Perham RN, Stribling D (1978). "Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);633-41. PMID: 417719

Berger90: Berger SA, Evans PR (1990). "Active-site mutants altering the cooperativity of E. coli phosphofructokinase." Nature 343(6258);575-6. PMID: 2137204

Berger91: Berger SA, Evans PR (1991). "Steady-state fluorescence of Escherichia coli phosphofructokinase reveals a regulatory role for ATP." Biochemistry 1991;30(34);8477-80. PMID: 1832014

Berger92: Berger SA, Evans PR (1992). "Site-directed mutagenesis identifies catalytic residues in the active site of Escherichia coli phosphofructokinase." Biochemistry 31(38);9237-42. PMID: 1390710

Berry93: Berry A, Marshall KE (1993). "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli." FEBS Lett 318(1);11-6. PMID: 8436219

Blangy68: Blangy D, Buc H, Monod J (1968). "Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli." J Mol Biol 31(1);13-35. PMID: 4229913

Blangy68a: Blangy D (1968). "Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme." FEBS Lett 2(2);109-111. PMID: 11946283

Blom96: Blom NS, Tetreault S, Coulombe R, Sygusch J (1996). "Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase." Nat Struct Biol 3(10);856-62. PMID: 8836102

Bock66: Bock A, Neidhardt FC (1966). "Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase." J Bacteriol 92(2);470-6. PMID: 16562137

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc11.