If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: ED pathway
|Superclasses:||Degradation/Utilization/Assimilation → Carbohydrates Degradation → Sugars Degradation → Entner-Duodoroff Pathways|
|Generation of Precursor Metabolites and Energy → Entner-Duodoroff Pathways|
The Entner-Doudoroff pathway joins the pentose phosphate pathway (oxidative branch) to glycolysis via two steps, catalyzed by inducible enzymes.
This pathway is important to E. coli because sugar acids, which are significant nutrients in both of its habitats, intestinal and aquatic, are metabolized via this pathway. Strains that are mutationally blocked in this pathway are unable to grow on gluconate, glucuronate, or galacturonate and are also unable to colonize the mouse intestine [Sweeney96]. The uronic acids feed into the pathway's sole intermediate, 2-keto-3-deoxy-6-phospho-gluconate so the dependence of their metabolism on an intact Entner-Doudoroff pathway is clear [Peekhaus98]. The dependence of gluconate's metabolism on an intact Entner-Doudoroff pathway is less obvious because it is also metabolized via the pentose phosphate pathway.
Enzymes of the Entner-Doudoroff pathway are induced by growth on gluconate, glucuronate, or methyl-β-D-glucuronide; phosphate or carbon limitation [Murray05].
Superpathways: superpathway of glycolysis and Entner-Doudoroff
Sweeney96: Sweeney NJ, Laux DC, Cohen PS (1996). "Escherichia coli F-18 and E. coli K-12 eda mutants do not colonize the streptomycin-treated mouse large intestine." Infect Immun 64(9);3504-11. PMID: 8751891
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
Egan92: Egan SE, Fliege R, Tong S, Shibata A, Wolf RE, Conway T (1992). "Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon." J Bacteriol 1992;174(14);4638-46. PMID: 1624451
Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726
LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532
Patil92: Patil RV, Dekker EE (1992). "Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene." J Bacteriol 1992;174(1);102-7. PMID: 1339418
Pouyssegur71: Pouyssegur JM, Stoeber FR (1971). "[The common degradative pathway for hexuronates in Escherichia coli K 12. Purification, properties and individuality of 2-keto-3-deoxy-6-phospho-D-gluconate aldolase]." Eur J Biochem 1971;21(3);363-73. PMID: 4936448
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
Walters08: Walters MJ, Srikannathasan V, McEwan AR, Naismith JH, Fierke CA, Toone EJ (2008). "Characterization and crystal structure of Escherichia coli KDPGal aldolase." Bioorg Med Chem 16(2):710-20. PMID: 17981470
Wang81: Wang JK, Dekker EE, Lewinski ND, Winter HC "Physical and chemical evidence for the trimeric subunit structure of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli K-12." J Biol Chem 1981;256:1793-1800.
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493