If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: pentose shunt, hexose monophosphate shunt, phosphogluconate pathway, superpathway of oxidative and non-oxidative branches of pentose phosphate pathway
|Superclasses:||Generation of Precursor Metabolites and Energy → Pentose Phosphate Pathways|
The pentose phosphate pathway is one of the three essential pathways of central metabolism. It supplies three of E. coli's 13 precursor metabolites (compounds needed for the biosyntheses): D-ribose-5-phosphate, sedoheptulose-7-phosphate, and erythrose-4-phosphate. Regardless of the carbon source upon which E. coli is growing, some carbon must flow through the pentose phosphate pathway to meet the cell's requirements for these metabolites. In addition, this pathway is an important source of reducing equivalents in the form of NADPH, which is also needed for biosyntheses. The pathway begins with one intermediate of glycolysis, glucose-6-phosphate, and ends with the formation of two others, fructose-6-phosphate and D-glyceraldehyde-3-phosphate.
For convenience, the pentose phosphate pathway is commonly divided into its preliminary oxidative portion, in which glucose-6-phosphate is oxidized to ribulose-5-phosphate, and its subsequent non-oxidative portion in which, through a series of transaldolase and transketolase reactions, ribulose-5-phosphate is converted into fructose-6-phosphate and glyceraldehyde-3-phosphate.
Acebron09: Acebron SP, Martin I, del Castillo U, Moro F, Muga A (2009). "DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface." FEBS Lett 583(18);2991-6. PMID: 19698713
Asztalos07: Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G, Tittmann K (2007). "Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate." Biochemistry 46(43);12037-52. PMID: 17914867
Aucamp08: Aucamp JP, Martinez-Torres RJ, Hibbert EG, Dalby PA (2008). "A microplate-based evaluation of complex denaturation pathways: structural stability of Escherichia coli transketolase." Biotechnol Bioeng 99(6);1303-10. PMID: 17969139
Avison01: Avison MB, Horton RE, Walsh TR, Bennett PM (2001). "Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media." J Biol Chem 276(29);26955-61. PMID: 11350954
Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043
Chandran03: Chandran SS, Yi J, Draths KM, von Daeniken R, Weber W, Frost JW (2003). "Phosphoenolpyruvate availability and the biosynthesis of shikimic acid." Biotechnol Prog 19(3);808-14. PMID: 12790643
Chang95: Chang JT, Green CB, Wolf RE (1995). "Inhibition of translation initiation on Escherichia coli gnd mRNA by formation of a long-range secondary structure involving the ribosome binding site and the internal complementary sequence." J Bacteriol 177(22);6560-7. PMID: 7592434
Chen10b: Chen YY, Ko TP, Chen WH, Lo LP, Lin CH, Wang AH (2010). "Conformational changes associated with cofactor/substrate binding of 6-phosphogluconate dehydrogenase from Escherichia coli and Klebsiella pneumoniae: Implications for enzyme mechanism." J Struct Biol 169(1);25-35. PMID: 19686854
David70: David J, Wiesmeyer H (1970). "Regulation of ribose metabolism in Escherichia coli. II. Evidence for two ribose-5-phosphate isomerase activities." Biochim Biophys Acta 208(1);56-67. PMID: 4909663
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Domain07: Domain F, Bina XR, Levy SB (2007). "Transketolase A, an enzyme in central metabolism, derepresses the marRAB multiple antibiotic resistance operon of Escherichia coli by interaction with MarR." Mol Microbiol 66(2);383-94. PMID: 17850260
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