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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The enzyme Trehalase is a glycoside hydrolase, produced by cells in the brush border of the small intestine, which catalyzes the conversion of trehalose to glucose. It is found in most animals.
The non-reducing disaccharide trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is one of the most important storage carbohydrates, and is produced by almost all forms of life except mammals. The disaccharide is hydrolyzed into two molecules of glucose by the enzyme trehalase. There are two types of trehalases found in Saccharomyces cerevisiae, viz. neutral trehalase (NT) and acid trehalase (AT) classified according to their pH optima [4]. NT has an optimum pH of 7.0, while that of AT is 4.5.
Recently it has been reported that more than 90% of total AT activity in S. cerevisiae is extracellular and cleaves extracellular trehalose into glucose in the periplasmic space.