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Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Pathway: L-rhamnose degradation I

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Genetic Regulation Schematic: ?

Synonyms: rhamnose catabolism, rhamnose degradation

Superclasses: Degradation/Utilization/Assimilation Carbohydrates Degradation Sugars Degradation L-rhamnose Degradation

Summary:
Via reactions catalyzed by proteins encoded in linked operons comprising a regulon, the methylpentose, rhamnose, is taken into the cell and metabolized, enabling E. coli to grow on it as a total source of carbon and energy. An isomerase and subsequent kinase convert rhamnose to rhamnulose-1-phosphate, which is cleaved by a specific aldolase into dihydroxyacetone phosphate (an intermediate of glycolysis, which thereby enters central metabolism), and (S)-lactaldehyde. L-fucose, the other methylpentose that E. coli can utilize, is metabolized by an analogous series of reactions (see fucose degradation).

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. E. 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

Credits:
Created 09-Sep-1994 by Riley M , Marine Biological Laboratory
Revised 09-Jun-2006 by Ingraham JL , UC Davis
Revised 24-Oct-2007 by Keseler I , SRI International


References

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

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

Badia89: Badia J, Baldoma L, Aguilar J, Boronat A (1989). "Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12." FEMS Microbiol Lett 53(3);253-7. PMID: 2558952

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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Chiu64: Chiu TH, Feingold DS (1964). "The purification and properties of L-rhamnulokinase." Biochim Biophys Acta 92;489-97. PMID: 14264882

Chiu64a: Chiu TH, Feingold D "Purification and properties of L-Rhamnulokinase." B B Acta 1964;92:489-497.

Chiu65: Chiu TH, Feingold DS (1965). "Substrate specificity of L-rhamnulose 1-phosphate aldolase." Biochem Biophys Res Commun 19;511-6. PMID: 14339000

Chiu69: Chiu TH, Feingold DS (1969). "L-rhamnulose 1-phosphate aldolase from Escherichia coli. Crystallization and properties." Biochemistry 1969;8(1);98-108. PMID: 4975916

Chiu75: Chiu TH, Evans KL, Feingold DS (1975). "L-Rhamnulose-1-phosphate aldosase." Methods Enzymol 1975;42;364-9. PMID: 237196

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

Fessner92: Fessner WD, Badia J, Eyrisch O, Schneider A, Sinerius G (1992). "Enzymatic syntheses of rare ketose 1-phosphates." Tetrahedron Letters 33;2231-2234.

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Grueninger06: Grueninger D, Schulz GE (2006). "Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli." J Mol Biol 359(3);787-97. PMID: 16674975

Grueninger07: Grueninger D, Schulz GE (2007). "Substrate spectrum of l-rhamnulose kinase related to models derived from two ternary complex structures." FEBS Lett 581(16);3127-30. PMID: 17568582

Grueninger08: Grueninger D, Schulz GE (2008). "Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase." Biochemistry 47(2);607-14. PMID: 18085797

Grueninger08a: Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE (2008). "Designed protein-protein association." Science 319(5860);206-9. PMID: 18187656

Hixon96: Hixon M, Sinerius G, Schneider A, Walter C, Fessner WD, Schloss JV (1996). "Quo vadis photorespiration: a tale of two aldolases." FEBS Lett 392(3);281-4. PMID: 8774862

Jimenez09: Jimenez A, Clapes P, Crehuet R (2009). "Protein flexibility and metal coordination changes in DHAP-dependent aldolases." Chemistry 15(6);1422-8. PMID: 19115296

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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