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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Article
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.