Alpha Galactosidase A Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| Attribute | Value | [@eng2007] |-----------|-------| [@waldek2013] | Protein Name | Alpha-Galactosidase A | | Gene Symbol | GLA | | UniProt ID | P06280 | | PDB Structures | 2VLW, 4AKH, 1R46, 5FEB | | Molecular Weight | 50.7 kDa (dimer: 101.4 kDa) | | Subcellular Localization | Lysosome | | Protein Family | Glycoside hydrolase family 27 |
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Overview
Alpha-Galactosidase A (α-Gal A) is a lysosomal hydrolase that catalyzes the hydrolysis of globotriaosylceramide (GL-3) and other glycolipids with terminal alpha-galactosyl residues.<sup>[1]</sup> Deficiency causes Fabry disease, an X-linked lysosomal storage disorder. Enzyme replacement therapy is available for treatment.
Structure
Quaternary Structure
Primary structure: 429 amino acids (including signal peptide)
Processed form: 398 amino acids (after signal peptide removal)
Quaternary: Homodimer
Glycosylation: N-linked glycans at positions 108, 146, 192
Substrate binding: Hydrophobic pocket for globotriaosylceramide
Specificity: Terminal α-galactosyl residues
PDB Structures
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Alpha-Galactosidase A Protein
Introduction
Alpha Galactosidase A Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| Attribute | Value | [@eng2007] |-----------|-------| [@waldek2013] | Protein Name | Alpha-Galactosidase A | | Gene Symbol | GLA | | UniProt ID | P06280 | | PDB Structures | 2VLW, 4AKH, 1R46, 5FEB | | Molecular Weight | 50.7 kDa (dimer: 101.4 kDa) | | Subcellular Localization | Lysosome | | Protein Family | Glycoside hydrolase family 27 |
</div>}
Overview
Alpha-Galactosidase A (α-Gal A) is a lysosomal hydrolase that catalyzes the hydrolysis of globotriaosylceramide (GL-3) and other glycolipids with terminal alpha-galactosyl residues.<sup>[1]</sup> Deficiency causes Fabry disease, an X-linked lysosomal storage disorder. Enzyme replacement therapy is available for treatment.
Structure
Quaternary Structure
Primary structure: 429 amino acids (including signal peptide)
Processed form: 398 amino acids (after signal peptide removal)
Quaternary: Homodimer
Glycosylation: N-linked glycans at positions 108, 146, 192
Biegstraaten M, et al. "Management goals for Fabry disease." Nat Rev Nephrol. 2015;11(11):678-687.
Background
The study of Alpha Galactosidase A Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
References
[@germain2010]: Germain DP. "Fabry disease." Orphanet J Rare Dis. 2010;5:30. PMID: 21146940(https://pubmed.ncbi.nlm.nih.gov/21146940/) [@schiffmann2009]: Schiffmann R, et al. "Enzyme replacement therapy in Fabry disease: A randomized controlled trial." JAMA. 2009;301(11):1137-1145. PMID: 19318652(https://pubmed.ncbi.nlm.nih.gov/19318652/) [@eng2007]: Eng CM, et al. "Safety and efficacy of agalsidase alfa in Fabry disease." Genet Med. 2007;9(9):605-612. PMID: 17873679(https://pubmed.ncbi.nlm.nih.gov/17873679/) [@waldek2013]: Waldek S, et al. "Agalsidase beta therapy for Fabry disease: 10-year experience." Mol Genet Metab. 2013;108(4):253-264. PMID: 23419421(https://pubmed.ncbi.nlm.nih.gov/23419421/)