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MetaCyc Pathway: trehalose degradation II (trehalase)
Traceable author statement to experimental supportInferred from experiment

Enzyme View:

Pathway diagram: trehalose degradation II (trehalase)

Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. 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/AssimilationCarbohydrates DegradationSugars DegradationTrehalose Degradation

Some taxa known to possess this pathway include : Apis mellifera, Escherichia coli K-12 substr. MG1655, Saccharomyces cerevisiae

Expected Taxonomic Range: Arthropoda, Bacteria , Fungi

General Background

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 (see trehalose 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).

In insects, trehalose is produced from fat body glycogen and is released into the hemolymph. In many insects, trehalose serves as an extracellular source of sugar via the action of trehalase, an enzyme widely distributed in insect tissues (reviewed in [Kramer05, Arrese10]).

About This Pathway

Trehalase enzymes hydrolyze a molecule of α,α-trehalose into two molecules of β-D-glucopyranose.

Escherichia coli K-12 can grow with trehalose as the sole carbon source, and employs different pathways for its degradation under different osmolarity conditions. Under high osmotic conditions external trehalose is hydrolyzed by periplasmic trehalase (TreA) [Boos87]. The resulting glucose molecules are then transported back into the cytoplasm through the glucose PTS [Styrvold91] (see trehalose degradation VI (periplasmic)).

A second trehalase, the cytoplasmic trehalase (TreF), is active during the transition period between high and low osmolarity. As the cells are shifting their metabolism to adjust to low osmolarity, TreF removes the internal pool of trehalose. The relatively low enzymatic activity of TreF is low enough not to compromise the biosynthesis of trehalose during high osmolarity, yet is sufficient to degrade the accumulated trehalose after the return to normal conditions, when no more biosynthesis occurrs [Horlacher96].

This trehalose degradation pathway is also used by the yeast Saccharomyces cerevisiae. This organism also has a cytoplasmic and a periplasmic trehalase enzymes [Kopp93]. Nth1p, the cytoplasmic enzyme, is required for the hydrolysis of intracellular trehalose, while Ath1p, the periplasmic enzyme, hydrolyzes extracellular trehalose [Jules04].

Superpathways: chitin biosynthesis

Variants: trehalose degradation I (low osmolarity), trehalose degradation III, trehalose degradation IV, trehalose degradation V, trehalose degradation VI (periplasmic)

Unification Links: EcoCyc:PWY0-1182

Created 31-Jan-2005 by Caspi R, SRI International
Revised 25-Mar-2010 by Keseler I, SRI International
Revised 23-Jan-2012 by Fulcher CA, SRI International


Arrese10: Arrese EL, Soulages JL (2010). "Insect fat body: energy, metabolism, and regulation." Annu Rev Entomol 55;207-25. PMID: 19725772

Boos87: Boos W, Ehmann U, Bremer E, Middendorf A, Postma P (1987). "Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions." J Biol Chem 1987;262(27);13212-8. PMID: 2820965

Horlacher96: Horlacher R, Uhland K, Klein W, Ehrmann M, Boos W (1996). "Characterization of a cytoplasmic trehalase of Escherichia coli." J Bacteriol 178(21);6250-7. PMID: 8892826

Jules04: Jules M, Guillou V, Francois J, Parrou JL (2004). "Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae." Appl Environ Microbiol 70(5);2771-8. PMID: 15128531

Kopp93: Kopp M, Muller H, Holzer H (1993). "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae." J Biol Chem 268(7);4766-74. PMID: 8444853

Kramer05: Kramer KJ, Muthukrishnan S (2005). "Chitin metabolism in insects." Comprehensive Molecular Insect Science (eds. L. I. Gilbert, K. Iatrou, and S. S. Gill) Elsevier, Vol. 4, 111-144.

Styrvold91: Styrvold OB, Strom AR (1991). "Synthesis, accumulation, and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase." J Bacteriol 173(3);1187-92. PMID: 1825082

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

Alajmo90: Alajmo E, de Meester W, Polli G (1990). "Facial nerve involvement: macroscopic and clinical evidence, therapeutic approach." Acta Otorhinolaryngol Ital 10 Suppl 29;35-42. PMID: 2177945

Albig88: Albig W, Entian KD (1988). "Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme." Gene 73(1);141-52. PMID: 3072253

Alizadeh96: Alizadeh P, Klionsky DJ (1996). "Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae." FEBS Lett 391(3);273-8. PMID: 8764988

App89: App H, Holzer H (1989). "Purification and characterization of neutral trehalase from the yeast ABYS1 mutant." J Biol Chem 264(29);17583-8. PMID: 2507544

Arguelles00: Arguelles JC (2000). "Physiological roles of trehalose in bacteria and yeasts: a comparative analysis." Arch Microbiol 174(4);217-24. PMID: 11081789

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

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Cardona09: Cardona F, Parmeggiani C, Faggi E, Bonaccini C, Gratteri P, Sim L, Gloster TM, Roberts S, Davies GJ, Rose DR, Goti A (2009). "Total syntheses of casuarine and its 6-O-alpha-glucoside: complementary inhibition towards glycoside hydrolases of the GH31 and GH37 families." Chemistry 15(7);1627-36. PMID: 19123216

Crowe94: Crowe LM, Spargo BJ, Ioneda T, Beaman BL, Crowe JH (1994). "Interaction of cord factor (alpha, alpha'-trehalose-6,6'-dimycolate) with phospholipids." Biochim Biophys Acta 1194(1);53-60. PMID: 8075141

Curtis75: Curtis SJ, Epstein W (1975). "Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase." J Bacteriol 122(3);1189-99. PMID: 1097393

Dai99a: Dai N, Schaffer A, Petreikov M, Shahak Y, Giller Y, Ratner K, Levine A, Granot D (1999). "Overexpression of Arabidopsis hexokinase in tomato plants inhibits growth, reduces photosynthesis, and induces rapid senescence." Plant Cell 11(7);1253-66. PMID: 10402427

De01: De Silva-Udawatta MN, Cannon JF (2001). "Roles of trehalose phosphate synthase in yeast glycogen metabolism and sporulation." Mol Microbiol 40(6);1345-56. PMID: 11442833

Destruelle95: Destruelle M, Holzer H, Klionsky DJ (1995). "Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity." Yeast 11(11);1015-25. PMID: 7502577

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


Franks87: Franks F. (1987). "Physical chemistry of small carbohydrates-equilibrium solution properties." Pure & Appl. Chem. Vol. 59, No. 9, pp. 1189-1202.

Fukuda83: Fukuda Y, Yamaguchi S, Shimosaka M, Murata K, Kimura A (1983). "Cloning of the glucokinase gene in Escherichia coli B." J Bacteriol 156(2);922-5. PMID: 6313627

Garre09: Garre E, Matallana E (2009). "The three trehalases Nth1p, Nth2p and Ath1p participate in the mobilization of intracellular trehalose required for recovery from saline stress in Saccharomyces cerevisiae." Microbiology 155(Pt 9);3092-9. PMID: 19520725

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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 19.5 on Fri Apr 29, 2016, BIOCYC11A.