Error: Pathway image not found.
D-Glucarate and D-Galactarate Degradation
Last Updated: 2018-12-21
Galactarate is a naturally occurring dicarboxylic acid analog of D-galactose. E. coli can use both diacid sugars galactarate and D-glucarate as the sole source of carbon for growth. The initial step in the degradation of galactarate is its dehydration to 5-dehydro-4-deoxy-D-glucarate(2--) by galactarate dehydratase. Glucaric acid can also be dehydrated by a glucarate dehydratase resulting in water and 5-dehydro-4-deoxy-D-glucarate(2--). The 5-dehydro-4-deoxy-D-glucarate(2--) is then metabolized by a alpha-dehydro-beta-deoxy-D-glucarate aldolase resulting in pyruvic acid and a tartonate semialdehyde. Pyruvic acid interacts with coenzyme A through a NAD driven Pyruvate dehydrogenase complex resulting in a carbon dioxide, an NADH and an acetyl-CoA. The tartronate semialdehyde interacts with a hydrogen ion through a NADPH driven tartronate semialdehyde reductase resulting in a NADP and a glyceric acid. The glyceric acid is phosphorylated by an ATP-driven glycerate kinase 2 resulting in an ADP, a hydrogen ion and a 2-phosphoglyceric acid. The latter compound is dehydrated by an enolase resulting in the release of water and a phosphoenolpyruvic acid. The phosphoenolpyruvic acid interacts with a hydrogen ion through an ADP driven pyruvate kinase resulting in an ATP and a pyruvic acid. The pyruvic acid then interacts with water and an ATP through a phosphoenolpyruvate synthetase resulting in the release of a hydrogen ion, a phosphate, an AMP and a Phosphoenolpyruvic acid.
D-Glucarate and D-Galactarate Degradation References
Blackwell NC, Cullis PM, Cooper RA, Izard T: Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1368-9.Pubmed: 10393309
Blumenthal HJ, Jepson T: Asymmetric dehydration of galactarate by bacterial galactarate dehydratase. Biochem Biophys Res Commun. 1964 Oct 14;17(3):282-7.Pubmed: 4285952
Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA: Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry. 1998 Oct 13;37(41):14369-75. doi: 10.1021/bi981124f.Pubmed: 9772162
Izard T, Blackwell NC: Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism. EMBO J. 2000 Aug 1;19(15):3849-56. doi: 10.1093/emboj/19.15.3849.Pubmed: 10921867
Monterrubio R, Baldoma L, Obradors N, Aguilar J, Badia J: A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli. J Bacteriol. 2000 May;182(9):2672-4.Pubmed: 10762278
Njau RK, Herndon CA, Hawes JW: Novel beta -hydroxyacid dehydrogenases in Escherichia coli and Haemophilus influenzae. J Biol Chem. 2000 Dec 8;275(49):38780-6. doi: 10.1074/jbc.M007432200.Pubmed: 10978349
Ornston MK, Ornston LN: Two forms of D-glycerate kinase in Escherichia coli. J Bacteriol. 1969 Mar;97(3):1227-33.Pubmed: 4887503
Rea D, Hovington R, Rakus JF, Gerlt JA, Fulop V, Bugg TD, Roper DI: Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry. 2008 Sep 23;47(38):9955-65. doi: 10.1021/bi800943g. Epub 2008 Aug 29.Pubmed: 18754683
Roberton AM, Sullivan PA, Jones-Mortimer MC, Kornberg HL: Two genes affecting glucarate utilization in Escherichia coli K12. J Gen Microbiol. 1980 Apr;117(2):377-82. doi: 10.1099/00221287-117-2-377.Pubmed: 6999115
Highlighted elements will appear in red.
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data