KOPS - Das Institutionelle Repositorium der Universität Konstanz

Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme

Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:6faaec32efce2641470d34d425b5c1a9

POLLEGIONI, Loredano, Sandro GHISLA, Mirella S. PILONE, 1992. Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme. In: Biochemical Journal. 286(2), pp. 389-394. ISSN 0264-6021. eISSN 1470-8728. Available under: doi: 10.1042/bj2860389

@article{Pollegioni1992Studi-8219, title={Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme}, year={1992}, doi={10.1042/bj2860389}, number={2}, volume={286}, issn={0264-6021}, journal={Biochemical Journal}, pages={389--394}, author={Pollegioni, Loredano and Ghisla, Sandro and Pilone, Mirella S.} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8219"> <dcterms:issued>1992</dcterms:issued> <dcterms:abstract xml:lang="eng">D-Amino acid oxidase (EC 1.4.3.3) from Rhodotorula gracilis has been reconstituted with 8-chloro-, 8-mercapto-, 6-hydroxy-, 2-thio-, 5-deaza- and 1-deaza-FAD, and the properties of the resulting complexes have been studied and compared with those of the correspondingly modified pig kidney D-amino acid oxidases. Binding appears to be tight for most analogues, at least as tight as for native FAD (~10(-8) M). 8-Mercapto- and 6-hydroxy-FAD bind in their para- and ortho-quinoid forms respectively to yeast D-amino acid oxidase, inferring the presence of a positive charge near the flavin N(1) position, as in the case of the mammalian enzyme. On the other hand, important differences in active-site microenvironment emerge: solvent accessibility to flavin position 8 is drastically restricted in yeast D-amino acid oxidase as indicated by the unreactivity of 8-chloro- and 8-mercapto-FAD enzyme with thiolates and alkylating agents. Significantly different microenvironments are also likely to occur around the flavin positions N(1)-C(2) = 0, N(3)-H and N(5). This is deduced from the differences in interaction of the two proteins with 1-deaza-FAD, 5-deaza-FAD and 2-thio-FAD and from the properties of the respective complexes. The same re-side flavin stereospecificity as shown by the mammalian enzyme was determined for the yeast enzyme using 8-hydroxy-5-deaza-FAD. Thus we can deduce the presence of a similar pattern of functional groups at the active centres of the two enzymes, while the fine tuning of specificity and regulation correlate with environmental differences at specific flavin loci.</dcterms:abstract> <dc:language>eng</dc:language> <dcterms:bibliographicCitation>First publ. in: Biochemical Journal ; 286 (1992). - S. 389-394</dcterms:bibliographicCitation> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:format>application/pdf</dc:format> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8219"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8219/1/Studies_on_the_active_centre_of_Rhodotorula_gracilis_D_amino_acid_oxidase_and_comparison_with_pig_kidney_enzyme.pdf"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:31Z</dcterms:available> <dc:contributor>Pollegioni, Loredano</dc:contributor> <dc:creator>Pilone, Mirella S.</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8219/1/Studies_on_the_active_centre_of_Rhodotorula_gracilis_D_amino_acid_oxidase_and_comparison_with_pig_kidney_enzyme.pdf"/> <dc:contributor>Ghisla, Sandro</dc:contributor> <dcterms:title>Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme</dcterms:title> <dc:creator>Ghisla, Sandro</dc:creator> <dc:creator>Pollegioni, Loredano</dc:creator> <dc:contributor>Pilone, Mirella S.</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:31Z</dc:date> <dc:rights>deposit-license</dc:rights> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Studies_on_the_active_centre_of_Rhodotorula_gracilis_D_amino_acid_oxidase_and_comparison_with_pig_kidney_enzyme.pdf 132

Das Dokument erscheint in:

deposit-license Solange nicht anders angezeigt, wird die Lizenz wie folgt beschrieben: deposit-license

KOPS Suche


Stöbern

Mein Benutzerkonto