MetaCyc Pathway: glucose and glucose-1-phosphate degradation
Inferred from experiment

Pathway diagram: glucose and glucose-1-phosphate degradation

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationCarbohydrates DegradationSugars Degradation

Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655

Expected Taxonomic Range: Archaea, Bacteria , Eukaryota

General Background

It is well known that Escherichia coli can use glucose as a sole source of carbon and energy. The D isomer of glucose is widely found in nature and D-glucopyranose is predominant in aqueous solution [Franks87]. Exogenous D-glucopyranose enters the cell through outer membrane porins and is then actively transported into the cell via the inner membrane phosphotransferase system (PTS) which transforms it into D-glucopyranose 6-phosphate as it crosses the cell membrane. D-glucopyranose 6-phosphate is also produced biosynthetically during gluconeogenesis. D-glucopyranose 6-phosphate is one of the basic precursor metabolites for biosynthetic pathways. It is also a substrate for the central degradative pathways glycolysis and the pentose phosphate cycle.

Escherichia coli can also grow on exogenously supplied glucose-1-phosphate (minimal medium containing glucose 1-phosphate) as sole carbon source [Pradel91]. Endogenous α-D-glucopyranose 1-phosphate is an intermediate in the metabolism of glycogen and D-galactose. It is a building block for the sugar nucleotide UDP-α-D-glucose, which is used in some biosynthetic pathways. Reviewed by Mayer, C. and W. Boos in [ECOSAL] (see below).

About This Pathway

Substrates D-glucopyranose and α-D-glucopyranose 1-phosphate may be derived from exogenous sources, or endogenously produced, as indicated by the input pathway links. In general, the ability to utilize sugars and their modes of utilization are strain-dependent in Escherichia coli.

Exogenous β-D-glucopyranose uptake via the PTS curbs the utilization of other exogenous sugars, which is known as the glucose effect. This effect is lost if β-D-glucopyranose becomes limiting. Under these conditions β-D-glucopyranose can also enter the cell without phosphorylation, via outer membrane porins and the Mgl ABC transporter (not shown).

Endogenous β-D-glucopyranose can be produced by pathways for the degradation of glucose-containing disaccharides such as maltose (see pathway glycogen degradation I) α,α-trehalose, α-lactose and melibiose, as shown in the pathway links. In contrast to exogenous β-D-glucopyranose which is phosphorylated by the PTS, endogenous β-D-glucopyranose is phosphorylated by glucokinase before entering central metabolism, as shown in the pathway links (in [Meyer97]). More recently, a role for glucokinase and glucose in a complex regulatory mechanism for maltose utilization involving Glk, MalT, Mlc and PtsG has been proposed [Lengsfeld09].

It is possible that high levels of β-D-glucopyranose could accumulate inside the cell under certain conditions. It has been shown that the maltose acetyltransferase product of gene maa efficiently acetylates both maltose and β-D-glucopyranose (not shown). Evidence suggests that acetylation could be a detoxification mechanism in which acetylated β-D-glucopyranose diffuses from the cell [Boos81, Brand91].

There is evidence that β-D-glucopyranose can be oxidized to D-glucono-1,5-lactone (glucono-δ-lactone) by inner membrane glucose dehydrogenase. However, the fate of the D-glucono-1,5-lactone remains unclear. It has been reported that membrane vesicles from glucose-grown Escherichia coli oxidized glucose to gluconate in the presence of pyrroloquinoline quinone, a cofactor for glucose dehydrogenase [vanSchie85]. A gluconolactonase (EC has been partially characterized in Escherichia coli, but its D-gluconate product was not specifically identified [Hucho72] and no gene encoding this enzyme has been identified. D-gluconate can be degraded by a glucose utilization pathway that was described early [Cohen51], as shown in the pathway link. In addition, more recent work suggested possible excretion of D-gluconate although this compound was not specifically identified [Sashidhar10].

α-D-glucopyranose 1-phosphate is reversibly converted by phosphoglucomutase to α-D-glucose 6-phosphate. α-D-glucopyranose 1-phosphate is used in glycogen biosynthesis (see glycogen biosynthesis I (from ADP-D-Glucose)) and is produced during glycogen degradation (see glycogen degradation I). α-D-glucose 6-phosphate may spontaneously convert to β-D-glucose 6-phosphate in the physiological pH range [Salas65]. In addition, a glucose-6-phosphate 1-epimerase had been identified in Escherichia coli ATCC 9637 that could catalyze this production of β-D-glucose 6-phosphate.

Several phosphatases may catalyze the production of D-glucose (anomeric form unspecified) from α-D-glucopyranose 1-phosphate. The product of gene agp is a periplasmic enzyme that scavenges glucose and allows Escherichia coli to grow with glucose-1-phosphate as sole carbon source [Pradel91] and in [Lee03b].

Reviewed in Mayer, C. and W. Boos (2005) "Hexose/Pentose and Hexitol/Pentitol Metabolism." EcoSal module 3.4.1 [ECOSAL].

Unification Links: EcoCyc:GLUCOSE1PMETAB-PWY

Last-Curated 17-Mar-2010 by Fulcher CA, SRI International


Ball11: Ball S, Colleoni C, Cenci U, Raj JN, Tirtiaux C (2011). "The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis." J Exp Bot 62(6);1775-801. PMID: 21220783

Boos81: Boos W, Ferenci T, Shuman HA (1981). "Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli." J Bacteriol 1981;146(2);725-32. PMID: 7012137

Brand91: Brand B, Boos W (1991). "Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000." J Biol Chem 1991;266(21);14113-8. PMID: 1856235

Cohen51: Cohen SS (1951). "Utilization of gluconate and glucose in growing and virus-infected Escherichia coli." Nature 168(4278);746-7. PMID: 14882337

ECOSAL: EcoSal "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Franks87: Franks F. (1987). "Physical chemistry of small carbohydrates-equilibrium solution properties." Pure & Appl. Chem. Vol. 59, No. 9, pp. 1189-1202.

Hucho72: Hucho F, Wallenfels K (1972). "Glucono- -lactonase from Escherichia coli." Biochim Biophys Acta 1972;276(1);176-9. PMID: 4625870

Lee03b: Lee DC, Cottrill MA, Forsberg CW, Jia Z (2003). "Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase." J Biol Chem 278(33);31412-8. PMID: 12782623

Lengsfeld09: Lengsfeld C, Schonert S, Dippel R, Boos W (2009). "Glucose- and glucokinase-controlled mal gene expression in Escherichia coli." J Bacteriol 191(3);701-12. PMID: 19028900

Meyer97: Meyer D, Schneider-Fresenius C, Horlacher R, Peist R, Boos W (1997). "Molecular characterization of glucokinase from Escherichia coli K-12." J Bacteriol 179(4);1298-306. PMID: 9023215

Pradel91: Pradel E, Boquet PL (1991). "Utilization of exogenous glucose-1-phosphate as a source of carbon or phosphate by Escherichia coli K12: respective roles of acid glucose-1-phosphatase, hexose-phosphate permease, phosphoglucomutase and alkaline phosphatase." Res Microbiol 1991;142(1);37-45. PMID: 1648777

Salas65: Salas M, Vinuela E, Sols A (1965). "Spontaneous and enzymatically catalyzed anomerization of glucose 6-phosphate and anomeric specificity of related enzymes." J Biol Chem 240;561-8. PMID: 14275652

Sashidhar10: Sashidhar B, Inampudi KK, Guruprasad L, Kondreddy A, Gopinath K, Podile AR (2010). "Highly Conserved Asp-204 and Gly-776 Are Important for Activity of the Quinoprotein Glucose Dehydrogenase of Escherichia coli and for Mineral Phosphate Solubilization." J Mol Microbiol Biotechnol 18(2);109-119. PMID: 20215780

Shearer02: Shearer J, Graham TE (2002). "New perspectives on the storage and organization of muscle glycogen." Can J Appl Physiol 27(2);179-203. PMID: 12179957

vanSchie85: van Schie BJ, Hellingwerf KJ, van Dijken JP, Elferink MG, van Dijl JM, Kuenen JG, Konings WN (1985). "Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi)." J Bacteriol 163(2);493-9. PMID: 3926746

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

Accorsi89: Accorsi A, Piatti E, Piacentini MP, Gini S, Fazi A (1989). "Isoenzymes of phosphoglucomutase from human red blood cells: isolation and kinetic properties." Prep Biochem 19(3);251-71. PMID: 2533352

Adhya71: Adhya S, Schwartz M (1971). "Phosphoglucomutase mutants of Escherichia coli K-12." J Bacteriol 108(2);621-6. PMID: 4942754

Alajmo90: Alajmo E, de Meester W, Polli G (1990). "Facial nerve involvement: macroscopic and clinical evidence, therapeutic approach." Acta Otorhinolaryngol Ital 10 Suppl 29;35-42. PMID: 2177945

Albig88: Albig W, Entian KD (1988). "Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme." Gene 73(1);141-52. PMID: 3072253

Arora95: Arora KK, Pedersen PL (1995). "Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins." Arch Biochem Biophys 1995;319(2);574-8. PMID: 7786044

Asensio58: Asensio C, Sols A (1958). "Utilization and phosphorylation of sugars by Escherichia coli." Rev Esp Fisiol 14(4);269-75. PMID: 13658662

Asensio63: Asensio C, Avigad G, Horecker BL (1963). "Preferential galactose utilization in a mutant strain of E. coli." Arch Biochem Biophys 103;299-309. PMID: 14103281

Boles94: Boles E, Liebetrau W, Hofmann M, Zimmermann FK (1994). "A family of hexosephosphate mutases in Saccharomyces cerevisiae." Eur J Biochem 220(1);83-96. PMID: 8119301

Brautaset98: Brautaset T, Petersen S, Valla S (1998). "An experimental study on carbon flow in Escherichia coli as a function of kinetic properties and expression levels of the enzyme phosphoglucomutase." Biotechnol Bioeng 58(2-3);299-302. PMID: 10191405

Britton68: Britton HG, Clarke JB (1968). "The mechanism of the phosphoglucomutase reaction. Studies on rabbit muscle phosphoglucomutase with flux techniques." Biochem J 110(2);161-80. PMID: 5726186

CletonJansen90: Cleton-Jansen AM, Goosen N, Fayet O, van de Putte P (1990). "Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase." J Bacteriol 172(11);6308-15. PMID: 2228962

Constantinidou06: Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, Cole JA, Overton TW (2006). "A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth." J Biol Chem 281(8);4802-15. PMID: 16377617

Cottrill02: Cottrill MA, Golovan SP, Phillips JP, Forsberg CW (2002). "Inositol phosphatase activity of the Escherichia coli agp-encoded acid glucose-1-phosphatase." Can J Microbiol 48(9);801-9. PMID: 12455612

Cozier95: Cozier GE, Anthony C (1995). "Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens." Biochem J 312 ( Pt 3);679-85. PMID: 8554505

Cozier99: Cozier GE, Salleh RA, Anthony C (1999). "Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine." Biochem J 1999;340 ( Pt 3);639-47. PMID: 10359647

Csutora05: Csutora P, Strassz A, Boldizsar F, Nemeth P, Sipos K, Aiello DP, Bedwell DM, Miseta A (2005). "Inhibition of phosphoglucomutase activity by lithium alters cellular calcium homeostasis and signaling in Saccharomyces cerevisiae." Am J Physiol Cell Physiol 289(1);C58-67. PMID: 15703203

Curtis75: Curtis SJ, Epstein W (1975). "Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase." J Bacteriol 122(3);1189-99. PMID: 1097393

Dai99a: Dai N, Schaffer A, Petreikov M, Shahak Y, Giller Y, Ratner K, Levine A, Granot D (1999). "Overexpression of Arabidopsis hexokinase in tomato plants inhibits growth, reduces photosynthesis, and induces rapid senescence." Plant Cell 11(7);1253-66. PMID: 10402427

deJonge96: de Jonge R, Teixeira de Mattos MJ, Stock JB, Neijssel OM (1996). "Pyrroloquinoline quinone, a chemotactic attractant for Escherichia coli." J Bacteriol 178(4);1224-6. PMID: 8576064

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

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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