Glucosylceramidase cleaves the glucosidic bond of glucocerebroside to form ceramide

Stable Identifier
R-HSA-1605591
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Human glucosylceramidase (GBA) hydrolyses the glucosidic bond of glucocerebrosides to form ceramide (Dinur et al. 1986). GBA requires a low weight, non-enzymatic protein (one of the sphingolipids activator proteins) called Saposin-C (SAP-C) which acts with GBA to form an activated complex (Salvioli et al. 2000). Defects in GBA are the cause of Gaucher disease (GD) (MIM:230800), the most common glycolipid storage disorder, characterized by storage of glucocerebroside in the liver, spleen, and marrow (Beutler & Gelbart 1996).

Literature References
PubMed ID Title Journal Year
3456607 Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site

Dinur, T, Osiecki, KM, Legler, G, Gatt, S, Desnick, RJ, Grabowski, GA

Proc Natl Acad Sci U S A 1986
10781797 Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids

Salvioli, R, Tatti, M, Ciaffoni, F, Vaccaro, AM

FEBS Lett 2000
8889578 Glucocerebrosidase (Gaucher disease)

Beutler, E, Gelbart, T

Hum Mutat 1996
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
glucosylceramidase activity of GBA:SAPC [lysosomal membrane]
Physical Entity
Activity
Orthologous Events
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