ArticleThe Journal of biological chemistry2010
Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Historical Control Analysis Demonstrates Greater Long-Term Reduction in Plasma Globotriaosylceramide (Gb3) by Venglustat Compared With Placebo or Agalsidase Beta in Male Patients With Classic Fabry Disease.Molecular genetics & genomic medicine · 2025Trial
- Venglustat, an orally administered glucosylceramide synthase inhibitor: Assessment over 3 years in adult males with classic Fabry disease in an open-label phase 2 study and its extension study.Molecular genetics and metabolism · 2023Trial
- Synthetic Strategies for FRET-Enabled Carbohydrate Active Enzyme Probes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Fabry Disease: Molecular Basis, Pathophysiology, Diagnostics and Potential Therapeutic Directions.Biomolecules · 2021Review
- MultipleBBA clinical · 2017Article
- Lysosomal storage diseases.Translational science of rare diseases · 2017Review
- Human Alpha Galactosidases Transiently Produced inFrontiers in plant science · 2017Article
- Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.ACS chemical biology · 2016Article
- Article
- Pharmacological chaperones for human α-N-acetylgalactosaminidase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Fabry disease.Orphanet journal of rare diseases · 2010Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The human lysosomal enzymes alpha-galactosidase (alpha-GAL, EC 3.2.1.22) and alpha-N-acetylgalactosaminidase (alpha-NAGAL, EC 3.2.1.49) share 46% amino acid sequence identity and have similar folds. The active sites of the two enzymes share 11 of 13 amino acids, differing only where they interact with the 2-position of the substrates. Using a rational protein engineering approach, we interconverted the enzymatic specificity of alpha- GAL and alpha-NAGAL. The engineered alpha-GAL (which we call alpha-GAL(SA)) retains the antigenicity of alpha-GAL but has acquired the enzymatic specificity of alpha-NAGAL. Conversely, the engineered alpha-NAGAL (which we call alpha-NAGAL(EL)) retains the antigenicity of alpha-NAGAL but has acquired the enzymatic specificity of the alpha-GAL enzyme. Comparison of the crystal structures of the designed enzyme alpha-GAL(SA) to the wild-type enzymes shows that active sites of alpha-GAL(SA) and alpha-NAGAL superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.