Glucocerebrosidase

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Glucosidase, beta, acid
PBB Protein GBA image.jpg
Acid β-glucosidase, drawn from PDB 1OGS Proteopedia Acid-beta-glucosidase
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols GBA ; GBA1; GCB; GLUC
External IDs OMIM606463 MGI95665 HomoloGene68040 ChEMBL: 2179 GeneCards: GBA Gene
EC number 3.2.1.45
RNA expression pattern
PBB GE GBA 209093 s at tn.png
PBB GE GBA 210589 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2629 14466
Ensembl ENSG00000177628 ENSMUSG00000028048
UniProt P04062 P17439
RefSeq (mRNA) NM_000157 NM_001077411
RefSeq (protein) NP_000148 NP_001070879
Location (UCSC) Chr 1:
155.2 – 155.21 Mb
Chr 3:
89.2 – 89.21 Mb
PubMed search [1] [2]

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]

See also[edit]

References[edit]

  1. ^ "Entrez Gene: GBA glucosidase, beta; acid (includes glucosylceramidase)". 
  2. ^ "PDGene". Alzheimer Research Forum. 2008-11-12. Retrieved 2008-11-13. 
  3. ^ 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. 

Further reading[edit]

  • 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. 

External links[edit]