trehalase
Sign in to saveTrehalase enzymes are hydrolytic glycosidases, produced by most forms of life (except mammals), which catalyze the reduction of trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) - a non-reducing sugar and important storage carbohydrate - into glucose.
Research
1,534 papers- Trehalase inhibition by validamycin A may be a promising target to design new fungicides and insecticides.Pest management science · 2021
- Insect trehalase: physiological significance and potential applications.Glycobiology · 2015
- Elucidation of bacterial trehalose-degrading trehalase and trehalose phosphorylase: physiological significance and its potential applications.Glycobiology · 2024
- A trehalase-derived MAMP triggers LecRK-V-mediated immune responses in Arabidopsis.Science advances · 2025
- Trehalase inhibition in Helicoverpa armigera activates machinery for alternate energy acquisition.Journal of biosciences · 2024
via PubMed
Wikidata facts
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- EC enzyme number
- 3.2.1.28
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Encyclopedic overview
11 sectionsContents
- Function and classification
- Hydrolysis of trehalose
- Types of trehalase
- Neutral trehalase (NT)
- Acid Trehalase (AT)
- Occurrence and biological significance
- Bacteria
- Plants
- Fungi
- References
- See also
Trehalase enzymes are hydrolytic glycosidases, produced by most forms of life (except mammals), which catalyze the reduction of trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) - a non-reducing sugar and important storage carbohydrate - into glucose.
These enzymes are commonly found within brush border cells on the surface of the small intestine, and are present in most animals.
Excerpted from Wikipedia’s “trehalase” article, available under the CC BY-SA 4.0 licence.