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MetaCyc Pathway: superpathway of glycol metabolism and degradation

Enzyme View:

Pathway diagram: superpathway of glycol metabolism and 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/AssimilationAlcohols Degradation

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

Expected Taxonomic Range: Bacteria

Ethylene glycol has many applications commercially. It is used in antifreeze solutions and for the chemical synthesis of glyoxal, glycolate and glyoxylate. Glyoxylate is a building block for a variety of molecules of industrial interest. While Escherichia coli encodes the enzymes shown in this pathway by which it can degrade ethylene glycol to glyoxylate and subsequently 3-phosphoglycerate which can enter central metabolism through glycolysis, wild type cannot metabolize this alcohol at a sufficient rate to support growth. However, certain mutant strains with altered patterns of gene expression, can grow on ethylene glycol as a total source of carbon and energy. Some strains of Pseudomonas putida may also express all or part of this pathway and are hence able to metabolize ethylene glycol to glyoxylate or further [Muckschel12].

Subpathways: glycolate and glyoxylate degradation II, glycolate and glyoxylate degradation I, ethylene glycol degradation

Unification Links: EcoCyc:GLYCOL-GLYOXDEG-PWY

Revised 04-Oct-2012 by Weerasinghe D, SRI International


Muckschel12: Muckschel B, Simon O, Klebensberger J, Graf N, Rosche B, Altenbuchner J, Pfannstiel J, Huber A, Hauer B (2012). "Ethylene Glycol Metabolism of Pseudomonas putida." Appl Environ Microbiol. PMID: 23023748

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

ANALYSISREFEREN: Computational analysis, http://www.arabidopsis.org/servlets/TairObject?type=analysisreference&id=501719615.

Anstrom03: Anstrom DM, Kallio K, Remington SJ (2003). "Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution." Protein Sci 12(9);1822-32. PMID: 12930982

Autieri07: Autieri SM, Lins JJ, Leatham MP, Laux DC, Conway T, Cohen PS (2007). "L-fucose stimulates utilization of D-ribose by Escherichia coli MG1655 DeltafucAO and E. coli Nissle 1917 DeltafucAO mutants in the mouse intestine and in M9 minimal medium." Infect Immun 75(11);5465-75. PMID: 17709419

Badia91: Badia J, Gimenez R, Baldoma L, Barnes E, Fessner WD, Aguilar J (1991). "L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose." J Bacteriol 1991;173(16);5144-50. PMID: 1650346

Baldoma87: Baldoma L, Aguilar J (1987). "Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12." J Biol Chem 262(29);13991-6. PMID: 3308886

Baldoma88: Baldoma L, Aguilar J (1988). "Metabolism of L-fucose and L-rhamnose in Escherichia coli: aerobic-anaerobic regulation of L-lactaldehyde dissimilation." J Bacteriol 170(1);416-21. PMID: 3275622

Bari04: Bari R, Kebeish R, Kalamajka R, Rademacher T, Peterhansel C (2004). "A glycolate dehydrogenase in the mitochondria of Arabidopsis thaliana." J Exp Bot 55(397);623-30. PMID: 14966218

Bartsch08: Bartsch O, Hagemann M, Bauwe H (2008). "Only plant-type (GLYK) glycerate kinases produce d-glycerate 3-phosphate." FEBS Lett 582(20);3025-8. PMID: 18675808

Boronat79: Boronat A, Aguilar J (1979). "Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme." J Bacteriol 1979;140(2);320-6. PMID: 40956

Boronat81: Boronat A, Aguilar J (1981). "Metabolism of L-fucose and L-rhamnose in Escherichia coli: differences in induction of propanediol oxidoreductase." J Bacteriol 147(1);181-5. PMID: 7016842

Boronat83: Boronat A, Caballero E, Aguilar J (1983). "Experimental evolution of a metabolic pathway for ethylene glycol utilization by Escherichia coli." J Bacteriol 1983;153(1);134-9. PMID: 6336729

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Caballero83: Caballero E, Baldoma L, Ros J, Boronat A, Aguilar J (1983). "Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli." J Biol Chem 1983;258(12);7788-92. PMID: 6345530

Cabiscol90: Cabiscol E, Hidalgo E, Badia J, Baldoma L, Ros J, Aguilar J (1990). "Oxygen regulation of L-1,2-propanediol oxidoreductase activity in Escherichia coli." J Bacteriol 172(9);5514-5. PMID: 2203757

Cabiscol92: Cabiscol E, Badia J, Baldoma L, Hidalgo E, Aguilar J, Ros J (1992). "Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation." Biochim Biophys Acta 1118(2);155-60. PMID: 1730033

Cabiscol94: Cabiscol E, Aguilar J, Ros J (1994). "Metal-catalyzed oxidation of Fe2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis." J Biol Chem 269(9);6592-7. PMID: 8120011

Chang93: Chang YY, Wang AY, Cronan JE (1993). "Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-pyruvate oxidase family." J Biol Chem 1993;268(6);3911-9. PMID: 8440684

Chen83: Chen YM, Lin EC, Ros J, Aguilar J (1983). "Use of operon fusions to examine the regulation of the L-1,2-propanediol oxidoreductase gene of the fucose system in Escherichia coli K12." J Gen Microbiol 129(11);3355-62. PMID: 6319547

Chen84: Chen YM, Lin EC (1984). "Post-transcriptional control of L-1,2-propanediol oxidoreductase in the L-fucose pathway of Escherichia coli K-12." J Bacteriol 157(1);341-4. PMID: 6418721

Chen84a: Chen YM, Lin EC (1984). "Dual control of a common L-1,2-propanediol oxidoreductase by L-fucose and L-rhamnose in Escherichia coli." J Bacteriol 1984;157(3);828-32. PMID: 6421801

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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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