Trehalase
| trehalase (brush-border membrane glycoprotein) | |||||||
|---|---|---|---|---|---|---|---|
Trehalase | |||||||
| Identifiers | |||||||
| Symbol | TREH | ||||||
| NCBI gene | 11181 | ||||||
| HGNC | 12266 | ||||||
| OMIM | 275360 | ||||||
| RefSeq | NM_007180 | ||||||
| UniProt | O43280 | ||||||
| Other data | |||||||
| EC number | 3.2.1.28 | ||||||
| Locus | Chr. 11 q23.3 | ||||||
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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.
Two different trehalase enzymes have been isolated from Saccharomyces cerevisiae, and are classified according to the optimum working pH; where neutral trehalase (NT) has an optimum pH of 7.0, while that of acid trehalase (AT) is pH 4.5.
Recent studies of trehalase in S.cerevisiae have reported over 90% of AT activity is dedicated to extracellular cleavage of trehalose to glucose within the periplasmic space.