Reactome | GBA1:SAPC hydrolyzes GlcCer

GBA1:SAPC hydrolyzes GlcCer

Stable Identifier

R-HSA-1605591

Type

Reaction [transition]

Species

Homo sapiens

Compartment

lysosomal membrane, lysosomal lumen

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, Tatti, M, Ciaffoni, F, Vaccaro, AM	FEBS Lett	2000
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
8889578	Glucocerebrosidase (Gaucher disease) Beutler, E, Gelbart, T	Hum Mutat	1996