| http://purl.uniprot.org/citations/12686133 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12686133 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12686133 | http://www.w3.org/2000/01/rdf-schema#comment | "All pyrroloquinoline quinone (PQQ)-containing dehydrogenases whose structures are known contain Ca(2+) bonded to the PQQ at the active site. However, membrane glucose dehydrogenase (GDH) requires reconstitution with PQQ and Mg(2+) ions (but not Ca(2+)) for activity. To address the question of whether the Mg(2+) replaces the usual active site Ca(2+) in this enzyme, mutant GDHs were produced in which residues proposed to be involved in binding metal ion were modified (D354N-GDH and N355D-GDH and D354N-GDH/N355D-GDH). The most remarkable observation was that reconstitution with PQQ of the mutant enzymes was not supported by Mg(2+) ions as in the wild-type GDH, but it could be supported by Ca(2+), Sr(2+) or Ba(2+) ions. This was competitively inhibited by Mg(2+). This result, together with studies on the kinetics of the modified enzymes have led to the conclusion that, although a Ca(2+) ion is able to form part of the active site of the genetically modified GDH, as in all other PQQ-containing quinoproteins, a Mg(2+) ion surprisingly replaces Ca(2+) in the active site of the wild-type GDH."xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1570-9639(03)00041-4"xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12686133 |
| http://purl.uniprot.org/citations/12686133 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12686133 |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/author | "Anthony C."xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/author | "James P.L."xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/pages | "200-205"xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/title | "The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://purl.uniprot.org/core/volume | "1647"xsd:string |
| http://purl.uniprot.org/citations/12686133 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12686133 |
| http://purl.uniprot.org/citations/12686133 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12686133 |
| http://purl.uniprot.org/uniprot/P15877#attribution-92FBE1536E7FB8F83854BE7BE05C2E64 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/12686133 |
| http://purl.uniprot.org/enzyme/1.1.5.2 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12686133 |