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http://purl.uniprot.org/citations/20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20444686http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.118588"xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/author"Clark N.E."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/author"Garman S.C."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/author"Metcalf M.C."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/author"Guce A.I."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/author"Tomasic I.B."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/pages"21560-21566"xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/title"Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases."xsd:string
http://purl.uniprot.org/citations/20444686http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20444686http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20444686
http://purl.uniprot.org/citations/20444686http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20444686
http://purl.uniprot.org/uniprot/#_A0A0S3Q2A7-mappedCitation-20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20444686
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http://purl.uniprot.org/uniprot/#_P06280-mappedCitation-20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20444686
http://purl.uniprot.org/uniprot/#_Q53HF3-mappedCitation-20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20444686
http://purl.uniprot.org/uniprot/#_P17050-mappedCitation-20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20444686
http://purl.uniprot.org/uniprot/#_Q53Y83-mappedCitation-20444686http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20444686
http://purl.uniprot.org/uniprot/Q53HF3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20444686
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http://purl.uniprot.org/uniprot/P17050http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20444686