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.
Synonyms: fucose catabolism
|Superclasses:||Degradation/Utilization/Assimilation → Carbohydrates Degradation → Sugars Degradation|
Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655
Expected Taxonomic Range:
Via reactions catalyzed by proteins encoded in linked operons comprising a regulon, the methylpentose, fucose, is taken into the cell and metabolized, enabling Escherichia coli to grow on it as a total source of carbon and energy. An isomerase and subsequent kinase convert fucose to fuculose-1-phosphate, which is cleaved by a specific aldolase into glycerone phosphate (an intermediate of glycolysis, which thereby enters central metabolism), and (S)-lactaldehyde.
The enzymes of this pathway can be used for degradation of D-arabinose to glycerone phosphate and glycolaldehyde; see D-arabinose degradation I. L-rhamnose, the other methylpentose that Escherichia coli can utilize, is metabolized by an analogous series of reactions (see L-rhamnose degradation I).
Two pathways can be used for degradation of L-lactaldehyde. Aerobically, it is converted via lactate to pyruvate, also an intermediate of glycolysis. Anaerobically, lactaldehyde reductase is induced which converts lactaldehyde into propane-1,2-diol. Escherichia coli excretes propane-1,2-diol into the medium.
An overview of fucose and rhamnose degradation is shown in the superpathway of fucose and rhamnose degradation.
Review: Mayer, C. and W. Boos, Hexose/Pentose and Hexitol/Pentitol Metabolism. EcoSal Module 3.4.1 [ECOSAL]
Superpathways: superpathway of fucose and rhamnose degradation
Unification Links: EcoCyc:FUCCAT-PWY
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
Chang04a: 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
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
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
Grochowski06: Grochowski LL, Xu H, White RH (2006). "Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis." J Bacteriol 188(8);2836-44. PMID: 16585745
Joerger00: Joerger AC, Gosse C, Fessner WD, Schulz GE (2000). "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis." Biochemistry 39(20);6033-41. PMID: 10821675
Showing only 20 references. To show more, press the button "Show all references".
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493