Glucocerebrosidase

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Glucosidase, beta; acid (includes glucosylceramidase)
Acid β-glucosidase, drawn from PDB 1OGS.
Available structures: 1ogs, 1y7v, 2f61, 2j25, 2nsx, 2nt0, 2nt1
Identifiers
Symbol(s) GBA; GBA1; GCB; GLUC
External IDs OMIM: 606463 MGI: 95665 HomoloGene: 68040
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 2629 14466
Ensembl ENSG00000177628 ENSMUSG00000028048
Uniprot P04062 Q78NR7
Refseq NM_000157 (mRNA)
NP_000148 (protein)		 NM_001077411 (mRNA)
NP_001070879 (protein)
Location Chr 1: 153.47 - 153.48 Mb Chr 3: 89.29 - 89.29 Mb
Pubmed search [1] [2]

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'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]

[edit] See also

[edit] References

  1. ^ Entrez Gene: GBA glucosidase, beta; acid (includes glucosylceramidase).

[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. 

[edit] External links

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Hydrolase: sugar hydrolases (EC 3.2)
3.2.1: Glycoside hydrolases
3.2.2: Hydrolysing N-Glycosyl compounds
v • d • e
Metabolism: lipid metabolism - glycolipid/sphingolipid enzymes
To glycosphingolipid
To ceramide
To sphingosine
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