The 1.9 Å Structure of Human α- N -Acetylgalactosaminidase: The Molecular Basis of Schindler and Kanzaki Diseases
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 393, Issue: 2, Page: 435-447
2009
- 49Citations
- 72Captures
- 4Mentions
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Metrics Details
- Citations49
- Citation Indexes48
- 48
- CrossRef46
- Patent Family Citations1
- Patent Families1
- Captures72
- Readers72
- 72
- Mentions4
- References4
- Wikipedia4
Article Description
α- N -acetylgalactosaminidase (α-NAGAL; E.C. 3.2.1.49) is a lysosomal exoglycosidase that cleaves terminal α- N -acetylgalactosamine residues from glycopeptides and glycolipids. In humans, a deficiency of α-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease. To better understand the molecular defects in the diseases, we determined the crystal structure of human α-NAGAL after expressing wild-type and glycosylation-deficient glycoproteins in recombinant insect cell expression systems. We measured the enzymatic parameters of our purified wild-type and mutant enzymes, establishing their enzymatic equivalence. To investigate the binding specificity and catalytic mechanism of the human α-NAGAL enzyme, we determined three crystallographic complexes with different catalytic products bound in the active site of the enzyme. To better understand how individual defects in the α-NAGAL glycoprotein lead to Schindler disease, we analyzed the effect of disease-causing mutations on the three-dimensional structure.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0022283609009875; http://dx.doi.org/10.1016/j.jmb.2009.08.021; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=70349422116&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/19683538; https://linkinghub.elsevier.com/retrieve/pii/S0022283609009875
Elsevier BV
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