Glucocerebrosidase

Glucosidase, beta, acid
	; Acid β-glucosidase, drawn from PDB 1OGS Proteopedia Acid-beta-glucosidase
Available structures
PDB	1OGS, 1Y7V, 2F61, 2J25, 2NSX, 2NT0, 2NT1, 2V3D, 2V3E, 2V3F, 2WCG, 2WKL, 3GXD, 3GXF, 3GXI, 3GXM, 3KE0, 3KEH
Identifiers
Symbols	GBA; GBA1; GCB; GLUC
External IDs	OMIM: 606463 MGI: 95665 HomoloGene: 68040 GeneCards: GBA Gene
EC number	3.2.1.45
Gene Ontology
Molecular function	• glucosylceramidase activity; • protein binding; • hydrolase activity, acting on glycosyl bonds; • cation binding;
Cellular component	• lysosomal membrane; • membrane;
Biological process	• carbohydrate metabolic process; • lipid metabolic process; • sphingolipid metabolic process; • lysosome organization; • cell death;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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β-Glucocerebrosidase (also called acid β-glucosidase, D-glucosyl-N-acylsphingosine glucohydrolase, or GCase) is an enzyme with glucosylceramidase activity (EC 3.2.1.45) that is needed to cleave, by hydrolysis, the beta-glucosidic linkage of the chemical glucocerebroside, an intermediate in glycolipid metabolism. It is localized in the lysosome and has a molecular weight of 59700 Daltons.

Mutations in the glucocerebrosidase gene cause Gaucher's disease, a lysosomal storage disease characterized by an accumulation of glucocerebrosides. A related pseudogene is approximately 12 kb downstream of this gene on chromosome 1. Alternative splicing results in multiple transcript variants encoding the same protein.^[1]

In November 2008 mutations in the glucocerebrosidase gene were the mutations with the strongest association with Parkinson's disease in the PDGene database.^[2] The initial study that examined this link was published in 2004.^[3]

[edit] See also

Closely related enzymes
- GBA2: acid β-glucosidase (bile acid), also EC 3.2.1.45
- GBA3: acid β-glucosidase (cytosolic), EC 3.2.1.21
Recombinant glucocerebrosidases used as drugs

[edit] References

^ "Entrez Gene: GBA glucosidase, beta; acid (includes glucosylceramidase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2629.
^ "PDGene". Alzheimer Research Forum. 2008-11-12. http://www.pdgene.org/. Retrieved 2008-11-13.
^ Alicia Lwin, Eduard Orvisky, Ozlem Goker-Alpan, Mary E. LaMarca & Ellen Sidransky (January 2004). "Glucocerebrosidase mutations in subjects with parkinsonism". Molecular Genetics and Metabolism 81 (1): 70–3. doi:10.1016/j.ymgme.2003.11.004. PMID 14728994.

[edit] Further reading

Horowitz M, Zimran A (1994). "Mutations causing Gaucher disease". Hum. Mutat. 3 (1): 1–11. doi:10.1002/humu.1380030102. PMID 8118460.
Tayebi N, Stone DL, Sidransky E (2000). "Type 2 gaucher disease: an expanding phenotype". Mol. Genet. Metab. 68 (2): 209–19. doi:10.1006/mgme.1999.2918. PMID 10527671.
Stone DL, Tayebi N, Orvisky E et al (2000). "Glucocerebrosidase gene mutations in patients with type 2 Gaucher disease". Hum. Mutat. 15 (2): 181–8. doi:10.1002/(SICI)1098-1004(200002)15:2<181::AID-HUMU7>3.0.CO;2-S. PMID 10649495.
Caillaud C, Poenaru L (2002). "[Gaucher's and Fabry's diseases: biochemical and genetic aspects]". J. Soc. Biol. 196 (2): 135–40. PMID 12360742.
Fabrega S, Durand P, Mornon JP, Lehn P (2002). "[The active site of human glucocerebrosidase: structural predictions and experimental validations]". J. Soc. Biol. 196 (2): 151–60. PMID 12360744.
Alfonso P, Aznarez S, Giralt M et al (2007). "Mutation analysis and genotype/phenotype relationships of Gaucher disease patients in Spain". J. Hum. Genet. 52 (5): 391–6. doi:10.1007/s10038-007-0135-4. PMID 17427031.