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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Pathway: trehalose degradation I (low osmolarity)

Enzyme View:

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.

Superclasses: Degradation/Utilization/Assimilation Carbohydrates Degradation Sugars Degradation Trehalose Degradation

Some taxa known to possess this pathway include ? : Bacillus subtilis , Escherichia coli K-12 substr. MG1655 , Paenibacillus popilliae

Expected Taxonomic Range: Bacteria

Summary:
There are several alternative pathways for the degradation of trehalose. Depending on the organism, trehalose may enter the cell either through a permease, in which case it remains unmodified, or it may be transported by a phosphotransferase system (PTS), resulting in the phoshorylated trehalose-6-phosphate form. Degradation then proceeds by different mechanisms: Unmodified trehalose may be degraded by a hydrolyzing trehalase (see trehalose degradation II (trehalase)), or it may be split by the action of a trehalose phosphorylase (seetrehalose degradation IV and trehalose degradation V). Likewise, trehalose-6-phosphate may be either hydrolyzed by trehalose-6-phosphate hydrolase (see trehalose degradation I (low osmolarity)) or it could be attacked by a trehalose-6-phosphate phosphorylase (see trehalose degradation III).

Trehalose degradation utilizing a trehalose-6-phosphate is found in many bacteria. It was studied extensively in the Gram-negative bacterium Escherichia coli (under conditions of low osmolarity). However, it has also been demonstrated in some Gram-positive bacteria, including Paenibacillus popilliae and Bacillus subtilis [Bhumiratana74, Helfert95].

While Escherichia coli only synthesizes trehalose under conditions of high osmolarity, it can degrade the sugar under conditions of both low and high osmolarity. In fact, Escherichia coli can grow with trehalose as the sole carbon source. Different pathways are employed under different osmolarity conditions.

Since no trehalose biosynthesis is happening in low osmolarity conditions, the only source of trehalose is external supply. Trehalose is imported into the cell by a PTS system for trehalose, which is composed of the EIIAGlc of the glucose-PTS, and a trehalose-specific EIITre, encoded by the treB gene. Trehalose is phosphorylated during the transport and enters the cytoplasm as trehalose-6-phosphate.

The resulting trehalose-6-phosphate is then hydrolyzed by trehalose-6-phosphate hydrolase, which is encoded by the treC gene, yielding glucose and glucose-6-phosphate. The free glucose is phosphorylated further by glucokinase into a second molecule of glucose-6-phosphate, and both glucose-6-phosphate moieties enter glycolysis [Klein95, Rimmele94].

Variants: trehalose degradation II (trehalase) , trehalose degradation III , trehalose degradation IV , trehalose degradation V , trehalose degradation VI (periplasmic)

Unification Links: EcoCyc:TREDEGLOW-PWY

Credits:
Created 08-Oct-1996 by Riley M , Marine Biological Laboratory
Revised 10-Mar-2005 by Caspi R , SRI International


References

Bhumiratana74: Bhumiratana A, Anderson RL, Costilow RN (1974). "Trehalose metabolism by Bacillus popilliae." J Bacteriol 119(2);484-93. PMID: 4369400

Helfert95: Helfert C, Gotsche S, Dahl MK (1995). "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a phospho-alpha-(1-1)-glucosidase encoded by the treA gene." Mol Microbiol 16(1);111-120. PMID: 7651129

Klein95: Klein W, Horlacher R, Boos W (1995). "Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose." J Bacteriol 177(14);4043-52. PMID: 7608078

Rimmele94: Rimmele M, Boos W (1994). "Trehalose-6-phosphate hydrolase of Escherichia coli." J Bacteriol 1994;176(18);5654-64. PMID: 8083158

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

Arora95: Arora KK, Pedersen PL (1995). "Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins." Arch Biochem Biophys 1995;319(2);574-8. PMID: 7786044

ASENSIO58: ASENSIO C, SOLS A (1958). "Utilization and phosphorylation of sugars by Escherichia coli." Rev Esp Fisiol 14(4);269-75. PMID: 13658662

Asensio63: Asensio C, Avigad G, Horecker BL (1963). "Preferential galactose utilization in a mutant strain of E. coli." Arch Biochem Biophys 103;299-309. PMID: 14103281

Boos90: Boos W, Ehmann U, Forkl H, Klein W, Rimmele M, Postma P (1990). "Trehalose transport and metabolism in Escherichia coli." J Bacteriol 172(6);3450-61. PMID: 2160944

Decker99: Decker K, Gerhardt F, Boos W (1999). "The role of the trehalose system in regulating the maltose regulon of Escherichia coli." Mol Microbiol 32(4);777-88. PMID: 10361281

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

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."

Gotsche95: Gotsche S, Dahl MK (1995). "Purification and characterization of the phospho-alpha(1,1)glucosidase (TreA) of Bacillus subtilis 168." J Bacteriol 177(10);2721-6. PMID: 7751281

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kawai05: Kawai S, Mukai T, Mori S, Mikami B, Murata K (2005). "Hypothesis: structures, evolution, and ancestor of glucose kinases in the hexokinase family." J Biosci Bioeng 99(4);320-30. PMID: 16233797

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lengsfeld09: Lengsfeld C, Schonert S, Dippel R, Boos W (2009). "Glucose- and glucokinase-controlled mal gene expression in Escherichia coli." J Bacteriol 191(3);701-12. PMID: 19028900

Lunin04: Lunin VV, Li Y, Schrag JD, Iannuzzi P, Cygler M, Matte A (2004). "Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose." J Bacteriol 186(20);6915-27. PMID: 15466045

Magnani92: Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L (1992). "A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates." Biochem J 285 ( Pt 1);193-9. PMID: 1637300

Marechal84: Marechal LR (1984). "Transport and metabolism of trehalose in Escherichia coli and Salmonella typhimurium." Arch Microbiol 137(1);70-3. PMID: 6370169

Meyer97a: Meyer D, Schneider-Fresenius C, Horlacher R, Peist R, Boos W (1997). "Molecular characterization of glucokinase from Escherichia coli K-12." J Bacteriol 179(4);1298-306. PMID: 9023215

Miller07a: Miller BG (2007). "The mutability of enzyme active-site shape determinants." Protein Sci 16(9);1965-8. PMID: 17766388

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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
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC13A.