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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 3.2.1.28

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.2.1.28

Enzymes and Genes:
periplasmic trehalase Inferred from experiment : treA ( Escherichia coli K-12 substr. MG1655 )
cytoplasmic trehalase Inferred from experiment : treF ( Escherichia coli K-12 substr. MG1655 )
neutral trehalase Inferred from experiment : NTH2 ( Saccharomyces cerevisiae )
neutral trehalase Inferred from experiment : NTH1 ( Saccharomyces cerevisiae )
acid trehalase Inferred from experiment : ATH1 ( Saccharomyces cerevisiae )
trehalase (bound form) Inferred from experiment : LOC410795 ( Apis mellifera )

In Pathway: trehalose degradation II (trehalase) , trehalose degradation VI (periplasmic)

Reaction Locations: periplasmic space (sensu Gram-negative Bacteria), cytosol

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: α,α-trehalase

Enzyme Commission Synonyms: trehalase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.112976 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the α-glucosidic O-linkage of α,α-trehalose, releasing equimolar amounts of α- and β-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.

Citations: [Kalf58, Hehre82, Mori09]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:3.2.1.28 , ENZYME:EC:3.2.1.28 , IUBMB-ExplorEnz:EC:3.2.1.28 , KEGG:RELATED-TO:R00010 , UniProt:RELATED-TO:O43280 , UniProt:RELATED-TO:P13482 , UniProt:RELATED-TO:P19813 , UniProt:RELATED-TO:P32356 , UniProt:RELATED-TO:P32358 , UniProt:RELATED-TO:P32359 , UniProt:RELATED-TO:P35172 , UniProt:RELATED-TO:P48016 , UniProt:RELATED-TO:P62601 , UniProt:RELATED-TO:P78922

Credits:
Revised 01-Feb-2012 by Caspi R , SRI International


References

Hehre82: Hehre EJ, Sawai T, Brewer CF, Nakano M, Kanda T (1982). "Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with alpha- and beta-D-glucosyl fluoride." Biochemistry 21(13);3090-7. PMID: 7104311

Kalf58: Kalf GF, Rieder SV (1958). "The purification and properties of trehalase." J Biol Chem 230(2);691-8. PMID: 13525386

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

Mori09: Mori H, Lee JH, Okuyama M, Nishimoto M, Ohguchi M, Kim D, Kimura A, Chiba S (2009). "Catalytic reaction mechanism based on alpha-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase." Biosci Biotechnol Biochem 73(11);2466-73. PMID: 19897915


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 Fri Nov 28, 2014, BIOCYC13A.