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http://purl.uniprot.org/citations/10518528http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10518528http://www.w3.org/2000/01/rdf-schema#comment"Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter calcoaceticus is a classical quinoprotein. It requires the cofactor pyrroloquinoline quinone (PQQ) to catalyze the oxidation of glucose to gluconolactone. The precise catalytic role of PQQ in s-GDH and several other PQQ-dependent enzymes has remained controversial because of the absence of comprehensive structural data. We have determined the crystal structure of a ternary complex of s-GDH with PQQ and methylhydrazine, a competitive inhibitor of the enzyme. This complex, refined at 1.5-A resolution to an R factor of 16.7%, affords a detailed view of a cofactor-binding site of s-GDH. Moreover, it presents the first direct observation of covalent PQQ adduct in the active-site of a PQQ-dependent enzyme, thereby confirming previous evidence that the C5 carbonyl group of the cofactor is the most reactive moiety of PQQ."xsd:string
http://purl.uniprot.org/citations/10518528http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.21.11787"xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/author"Dijkstra B.W."xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/author"Rozeboom H.J."xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/author"Oubrie A."xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/pages"11787-11791"xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/title"Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex."xsd:string
http://purl.uniprot.org/citations/10518528http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10518528http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10518528
http://purl.uniprot.org/citations/10518528http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10518528
http://purl.uniprot.org/uniprot/#_P13650-mappedCitation-10518528http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10518528
http://purl.uniprot.org/uniprot/P13650http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10518528