If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: D-arabinose catabolism
|Superclasses:||Degradation/Utilization/Assimilation → Carbohydrates Degradation → Sugars Degradation → D-arabinose Degradation|
E. coli K-12 uses the enzymes of the fucose degradation pathway for utilization of D-arabinose. Expression of the enzymes in this pathway is normally induced by L-fucose and not by D-arabinose; thus, wild-type E. coli K-12 can not use D-arabinose as a sole source of carbon and energy without prior induction by growth on L-fucose [LeBlanc71]. Growth on D-arabinose requires a mutation in the transcriptional regulator FucR [Zhu86].
D-arabinose is metabolized yielding dihydroxy-acetone phosphate, an intermediate of glycolysis, which thereby enters central metabolism, and glycolaldehyde. Glycolaldehyde may be further catabolized to glycolate [LeBlanc71].
E. coli B uses a different pathway to catabolize D-arabinose; see D-arabinose degradation II.
Review: Mayer, C. and E. Boos, Hexose/Pentose and Hexitol/Pentitol Metabolism. EcoSal Module 3.4.1 [ECOSAL]
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
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
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
Chang04c: Chang DE, Smalley DJ, Tucker DL, Leatham MP, Norris WE, Stevenson SJ, Anderson AB, Grissom JE, Laux DC, Cohen PS, Conway T (2004). "Carbon nutrition of Escherichia coli in the mouse intestine." Proc Natl Acad Sci U S A 101(19);7427-32. PMID: 15123798
Di07a: Di Costanzo L, Gomez GA, Christianson DW (2007). "Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity." J Mol Biol 366(2);481-93. PMID: 17173928
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
Dreyer96: Dreyer MK, Schulz GE (1996). "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli." Acta Crystallogr D Biol Crystallogr 52(Pt 6);1082-91. PMID: 15299567
Franchini06: Franchini AG, Egli T (2006). "Global gene expression in Escherichia coli K-12 during short-term and long-term adaptation to glucose-limited continuous culture conditions." Microbiology 152(Pt 7);2111-27. PMID: 16804185
GarciaJunceda95: Garcia-Junceda E, Shen GJ, Sugai T, Wong CH (1995). "A new strategy for the cloning, overexpression and one step purification of three DHAP-dependent aldolases: rhamnulose-1-phosphate aldolase, fuculose-1-phosphate aldolase and tagatose-1,6-diphosphate aldolase." Bioorg Med Chem 3(7);945-53. PMID: 7582972
Showing only 20 references. To show more, press the button "Show all references".
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493