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MetaCyc Pathway: fucose degradation
Inferred from experiment

Pathway diagram: fucose 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.

Synonyms: fucose catabolism

Superclasses: Degradation/Utilization/AssimilationCarbohydrates DegradationSugars Degradation

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

Expected Taxonomic Range: Bacteria

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

Created 09-Sep-1994 by Riley M, Marine Biological Laboratory
Revised 09-May-2006 by Ingraham JL, UC Davis
Revised 31-Oct-2007 by Keseler I, SRI International


ECOSAL: EcoSal "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

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

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

Boulter73: Boulter JR, Gielow WO (1973). "Properties of D-arabinose isomerase purified from two strains of Escherichia coli." J Bacteriol 113(2);687-96. PMID: 4632320

Chang04: 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

Dreyer93: Dreyer MK, Schulz GE (1993). "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli." J Mol Biol 231(3);549-53. PMID: 8515438

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

Dreyer96a: Dreyer MK, Schulz GE (1996). "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure." J Mol Biol 259(3);458-66. PMID: 8676381

Fessner96: Fessner W-D, Schneider A, Held H, Sinerius G, Walter C, Hixon M, Schloss JV (1996). "The mechanism of Class II, metal-dependent aldolases." Angew Chem Int Ed Engl 35:2219-2221.

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

GarciaJunceda95a: Garcia-Junceda E, Shen GJ, Alajarin R, Wong CH (1995). "Cloning and overexpression of rhamnose isomerase and fucose isomerase." Bioorg Med Chem 3(10);1349-55. PMID: 8564401

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

Ghalambor62: Ghalambor MH, Heath EC (1962). "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate." J Biol Chem. Aug;237:2427-33. PMID: 13898172

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Green56: Green M, Cohen SS (1956). "Enzymatic conversion of L-fucose to L-fuculose." J Biol Chem 219(2);557-68. PMID: 13319278

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

Heath62: Heath EC, Ghalambor MA (1962). "Metabolism of L-fucose. I. The purification and properties of L-fuculose kinase." J Biol Chem 1962;237(8):2423-2426.

Herring03: Herring CD, Glasner JD, Blattner FR (2003). "Gene replacement without selection: regulated suppression of amber mutations in Escherichia coli." Gene 311;153-63. PMID: 12853150

Joerger00: Joerger AC, Mueller-Dieckmann C, Schulz GE (2000). "Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis." J Mol Biol 303(4);531-43. PMID: 11054289

Showing only 20 references. To show more, press the button "Show all references".

Report Errors or Provide Feedback
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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