GBA1:SAPC hydrolyzes GlcCer

Stable Identifier
R-HSA-1605591
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Human lysosomal glucosylceramidase (GBA1) hydrolyzes the glucosidic bond of glucocerebrosides (GlcCer) to form ceramide (Dinur et al. 1986). GBA1 requires a low-weight, non-enzymatic protein (one of the sphingolipids activator proteins) called Saposin-C (SAP-C) which acts with GBA1 to form an activated complex (Salvioli et al. 2000; Abdul-Hammed et al., 2017). Defects in GBA1 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
28126847 Lipids regulate the hydrolysis of membrane bound glucosylceramide by lysosomal β-glucocerebrosidase

Abdul-Hammed, M, Breiden, B, Schwarzmann, G, Sandhoff, K

J Lipid Res 2017
10781797 Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids

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

FEBS Lett 2000
3456607 Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site

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

Proc Natl Acad Sci U S A 1986
8889578 Glucocerebrosidase (Gaucher disease)

Gelbart, T, Beutler, E

Hum Mutat 1996
Participants
Participates
Catalyst Activity

glucosylceramidase activity of GBA1:SAPC [lysosomal membrane]

Orthologous Events
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