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Yeast trehalases: Two enzymes, one catalytic mission

Trehalose is a non-reducing disaccharide highly conserved throughout evolution. In yeasts, trehalose hydrolysis is confined to the enzyme trehalase, an α-glucosidase specific for trehalose as sole substrate. Two kinds of trehalase activity exist in yeasts: neutral and acid enzymes. This review makes...

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Published in:Biochimica et biophysica acta 2016-10, Vol.1860 (10), p.2249-2254
Main Authors: Maicas, Sergi, Guirao-Abad, José P., Argüelles, Juan-Carlos
Format: Article
Language:English
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Summary:Trehalose is a non-reducing disaccharide highly conserved throughout evolution. In yeasts, trehalose hydrolysis is confined to the enzyme trehalase, an α-glucosidase specific for trehalose as sole substrate. Two kinds of trehalase activity exist in yeasts: neutral and acid enzymes. This review makes a comparative survey of the main biochemical and genetic parameters, regulatory systems, tridimensional structure and catalytic mechanism of the two yeast trehalases. The yeast neutral and acid trehalases display sharp differences in biochemical features (optimum pH, Mr or amino acid sequence) physiological roles, subcellular location (cytosol vs vacuoles or cell wall) and regulatory control (phosphorylation vs catabolite repression). However, their identical specificity for trehalose is based on the presence of an (α/α)6 toroid folding structure in the active centre and a catalytic mechanism of anomeric inversion. This review expands our knowledge of the homology, functional features and catalytic mechanisms of α-glucosidases in yeasts. It provides a further analysis of the correlation between structures and predicted biological roles of macromolecules. •The hydrolysis of trehalose is confined in yeasts to the enzyme trehalase.•Two kinds of trehalase exist in yeasts: neutral (cytosolic) and acid (vacuolar or cell wall-linked) activities.•Both trehalases differ in biochemical parameters, physiological roles, regulatory mechanisms and tridimensional structure.•The yeasts trehalases share identical substrate specificity for trehalose.•The structure of the active centre and the catalytic mechanism are similar in neutral and acid trehalases.
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/j.bbagen.2016.04.020