Glucocerebrosidase

Glucosidase, beta; acid (includes glucosylceramidase)
Acid β-glucosidase, drawn from PDB: 1OGS​.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1ogs​, 1y7v​, 2f61​, 2j25​, 2nsx​, 2nt0​, 2nt1​
Identifiers
Symbols	GBA ; GBA1; GCB; GLUC
External IDs	Template:OMIM5 Template:MGI HomoloGene: 68040
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Glucocerebrosidase (also called glucosylceramidase, β-glucosidase, or D-glucosyl-N-acylsphingosine glucohydrolase) is an enzyme (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 gene cause Gaucher 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.

See also

• Imiglucerase
• Beta-glucosidase

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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

External links

• Glucocerebrosidase at the US National Library of Medicine Medical Subject Headings (MeSH)