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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:

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

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 direction in which it was curated.

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: ?

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 19.0 on Tue Sep 1, 2015, BIOCYC14B.