Distinguishing the differences in β-glycosylceramidase folds, dynamics, and actions informs therapeutic uses.

ABSTRACT: Glycosyl hydrolases (GHs) are carbohydrate-active enzymes that hydrolyze a specific β-glycosidic bond in glycoconjugate substrates; β-glucosidases degrade glucosylceramide, a ubiquitous glycosphingolipid. GHs are grouped into structurally similar families that themselves can be grouped into clans. GH1, GH5, and GH30 glycosidases belong to clan A hydrolases with a catalytic (β/α)₈ TIM barrel domain, whereas GH116 belongs to clan O with a catalytic (α/α)₆ domain. In humans, GH abnormalities underlie metabolic diseases. The lysosomal enzyme glucocerebrosidase (family GH30), deficient in Gaucher disease and implicated in Parkinson disease etiology, and the cytosol-facing membrane-bound glucosylceramidase (family GH116) remove the terminal glucose from the ceramide lipid m

SUBMITTER: Ben Bdira F 

PROVIDER: S-EPMC6277158 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature