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The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation

The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation

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UMHAU, Stephan, Loredano POLLEGIONI, Gianluca MOLLA, Kay DIEDERICHS, Wolfram WELTE, Mirella S. PILONE, Sandro GHISLA, 2000. The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. In: PNAS : Proceedings of the National Academy of Sciences of the United States of America. 97(23), pp. 12463-12468

@article{Umhau2000x-ray-7795, title={The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation}, year={2000}, number={23}, volume={97}, journal={PNAS : Proceedings of the National Academy of Sciences of the United States of America}, pages={12463--12468}, author={Umhau, Stephan and Pollegioni, Loredano and Molla, Gianluca and Diederichs, Kay and Welte, Wolfram and Pilone, Mirella S. and Ghisla, Sandro} }

<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/123456789/7795"> <dcterms:abstract xml:lang="deu">Flavin is one of the most versatile redox cofactors in nature and is used by many enzymes to perform a multitude of chemical reactions. D-Amino acid oxidase (DAAO), a member of the flavoprotein oxidase family, is regarded as a key enzyme for the understanding of the mechanism underlying flavin catalysis. The very highresolution structures of yeast DAAO complexed with D-alanine, D-trifluoroalanine, and L-lactate (1.20, 1.47, and 1.72 Å) provide strong evidence for hydride transfer as the mechanism of dehydrogenation. This is inconsistent with the alternative carbanion mechanism originally favored for this type of enzymatic reaction. The step of hydride transfer can proceed without involvement of amino acid functional groups. These structures, together with results from site-directed mutagenesis, point to orbital orientationysteering as the major factor in catalysis. A diatomic species, proposed to be a peroxide, is found at the active center and on the Re-side of the flavin. These results are of general relevance for the mechanisms of flavoproteins and lead to the proposal of a common dehydrogenation mechanism for oxidases and dehydrogenases.</dcterms:abstract> <dcterms:title>The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation</dcterms:title> <dc:creator>Diederichs, Kay</dc:creator> <dcterms:bibliographicCitation>First publ. in: PNAS [Proceedings of the National Academy of Sciences], Vol. 97 (2000), 23, pp. 12463-12468</dcterms:bibliographicCitation> <dc:creator>Umhau, Stephan</dc:creator> <dc:creator>Pilone, Mirella S.</dc:creator> <dc:contributor>Molla, Gianluca</dc:contributor> <dc:contributor>Umhau, Stephan</dc:contributor> <dc:contributor>Welte, Wolfram</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Welte, Wolfram</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7795"/> <dc:creator>Ghisla, Sandro</dc:creator> <dc:creator>Pollegioni, Loredano</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:36Z</dcterms:available> <dcterms:issued>2000</dcterms:issued> <dc:contributor>Diederichs, Kay</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:36Z</dc:date> <dc:language>eng</dc:language> <dc:format>application/pdf</dc:format> <dc:creator>Molla, Gianluca</dc:creator> <dc:contributor>Pollegioni, Loredano</dc:contributor> <dc:contributor>Pilone, Mirella S.</dc:contributor> </rdf:Description> </rdf:RDF>

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