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The structure of l-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site

The structure of l-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site

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PAWELEK, Peter D., Jaime CHEAH, René COULOMBE, Peter MACHEROUX, Sandro GHISLA, Alice VRIELINK, 2000. The structure of l-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. In: The EMBO Journal. 19(16), pp. 4204-4215. ISSN 0261-4189. eISSN 1460-2075

@article{Pawelek2000struc-8736, title={The structure of l-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site}, year={2000}, doi={10.1093/emboj/19.16.4204}, number={16}, volume={19}, issn={0261-4189}, journal={The EMBO Journal}, pages={4204--4215}, author={Pawelek, Peter D. and Cheah, Jaime and Coulombe, René and Macheroux, Peter and Ghisla, Sandro and Vrielink, Alice} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8736"> <dcterms:title>The structure of l-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site</dcterms:title> <dcterms:issued>2000</dcterms:issued> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:46:05Z</dc:date> <dc:contributor>Cheah, Jaime</dc:contributor> <dcterms:bibliographicCitation>First publ. in: The EMBO Journal 19 (2000), 16, pp. 4204-4215</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">The structure of l-amino acid oxidase (LAAO) from Calloselasma rhodostoma has been determined to 2.0 Å resolution in the presence of two ligands: citrate and o-aminobenzoate (AB). The protomer consists of three domains: an FAD-binding domain, a substrate-binding domain and a helical domain. The interface between the substrate-binding and helical domains forms a 25 Å long funnel, which provides access to the active site. Three AB molecules are visible within the funnel of the LAAO AB complex; their orientations suggest the trajectory of the substrate to the active site. The innermost AB molecule makes hydrogen bond contacts with the active site residues, Arg90 and Gly464, and the aromatic portion of the ligand is situated in a hydrophobic pocket. These contacts are proposed to mimic those of the natural substrate. Comparison of LAAO with the structure of mammalian d-amino acid oxidase reveals significant differences in their modes of substrate entry. Furthermore, a mirror-symmetrical relationship between the two substrate-binding sites is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the atoms involved in catalysis.</dcterms:abstract> <dc:contributor>Vrielink, Alice</dc:contributor> <dc:creator>Cheah, Jaime</dc:creator> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Pawelek, Peter D.</dc:contributor> <dc:contributor>Coulombe, René</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:46:05Z</dcterms:available> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Coulombe, René</dc:creator> <dc:creator>Macheroux, Peter</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:language>eng</dc:language> <dc:format>application/pdf</dc:format> <dc:contributor>Macheroux, Peter</dc:contributor> <dc:creator>Vrielink, Alice</dc:creator> <dc:creator>Pawelek, Peter D.</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8736"/> <dc:creator>Ghisla, Sandro</dc:creator> </rdf:Description> </rdf:RDF>

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