Alpha-galactosidase: Difference between revisions
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Revision as of 17:24, 18 August 2015
| Galactosidase, alpha | |||||||||||
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 PDB rendering based on 1r46. | |||||||||||
| Identifiers | |||||||||||
| Symbols | GLA ; GALA | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 55441 | ||||||||||
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| RNA expression pattern | |||||||||||
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| 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 | |||||||||
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]
Overview
Alpha-galactosidase is a glycoside hydrolase enzyme encoded by the GLA gene.
This gene encodes a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties.[1]
Pathology
A deficiency is associated with Fabry's disease.
See also
References
Further reading
- Naumoff DG (2004). "Phylogenetic analysis of α-galactosidases of the GH27 family". Molecular Biology (Engl Transl). 38 (3): 388–399. PMID 15285616. PDF
- Eng CM, Desnick RJ (1994). "Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene". Hum. Mutat. 3 (2): 103–11. doi:10.1002/humu.1380030204. PMID 7911050.
- Caillaud C, Poenaru L (2002). "[Gaucher's and Fabry's diseases: biochemical and genetic aspects]". J. Soc. Biol. 196 (2): 135–40. PMID 12360742.
- Germain DP (2002). "[Fabry's disease (alpha-galactosidase-A deficiency): physiopathology, clinical signs, and genetic aspects]". J. Soc. Biol. 196 (2): 161–73. PMID 12360745.
- Schaefer E, Mehta A, Gal A (2005). "Genotype and phenotype in Fabry disease: analysis of the Fabry Outcome Survey". Acta paediatrica (Oslo, Norway : 1992). Supplement. 94 (447): 87–92, discussion 79. PMID 15895718.
- Levin M (2006). "Fabry disease". Drugs Today. 42 (1): 65–70. doi:10.1358/dot.2006.42.1.957357. PMID 16511611.
- Lidove O, Joly D, Barbey F; et al. (2007). "Clinical results of enzyme replacement therapy in Fabry disease: a comprehensive review of literature". Int. J. Clin. Pract. 61 (2): 293–302. doi:10.1111/j.1742-1241.2006.01237.x. PMID 17263716.
- Dean KJ, Sweeley CC (1979). "Studies on human liver alpha-galactosidases. I. Purification of alpha-galactosidase A and its enzymatic properties with glycolipid and oligosaccharide substrates". J. Biol. Chem. 254 (20): 9994–10000. PMID 39940.
- Ishii S, Sakuraba H, Suzuki Y (1992). "Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease". Hum. Genet. 89 (1): 29–32. PMID 1315715.
- Ioannou YA, Bishop DF, Desnick RJ (1992). "Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion". J. Cell Biol. 119 (5): 1137–50. PMID 1332979.
- von Scheidt W, Eng CM, Fitzmaurice TF; et al. (1991). "An atypical variant of Fabry's disease with manifestations confined to the myocardium". N. Engl. J. Med. 324 (6): 395–9. PMID 1846223.
- Koide T, Ishiura M, Iwai K; et al. (1990). "A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser". FEBS Lett. 259 (2): 353–6. PMID 2152885.
- Kornreich R, Bishop DF, Desnick RJ (1990). "Alpha-galactosidase A gene rearrangements causing Fabry disease. Identification of short direct repeats at breakpoints in an Alu-rich gene". J. Biol. Chem. 265 (16): 9319–26. PMID 2160973.
- Sakuraba H, Oshima A, Fukuhara Y; et al. (1990). "Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease". Am. J. Hum. Genet. 47 (5): 784–9. PMID 2171331.
- Bernstein HS, Bishop DF, Astrin KH; et al. (1989). "Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene". J. Clin. Invest. 83 (4): 1390–9. PMID 2539398.
- Kornreich R, Desnick RJ, Bishop DF (1989). "Nucleotide sequence of the human alpha-galactosidase A gene". Nucleic Acids Res. 17 (8): 3301–2. PMID 2542896.
- Bishop DF, Kornreich R, Desnick RJ (1988). "Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region". Proc. Natl. Acad. Sci. U.S.A. 85 (11): 3903–7. PMID 2836863.
- Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH (1988). "A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A.". Gene. 58 (2–3): 177–88. PMID 2892762.
- Bishop DF, Calhoun DH, Bernstein HS; et al. (1986). "Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme". Proc. Natl. Acad. Sci. U.S.A. 83 (13): 4859–63. PMID 3014515.
- Lemansky P, Bishop DF, Desnick RJ; et al. (1987). "Synthesis and processing of alpha-galactosidase A in human fibroblasts. Evidence for different mutations in Fabry disease". J. Biol. Chem. 262 (5): 2062–5. PMID 3029062.
- Tsuji S, Martin BM, Kaslow DC; et al. (1987). "Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A.". Eur. J. Biochem. 165 (2): 275–80. PMID 3036505.
External links
- alpha-Galactosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.