| http://purl.uniprot.org/citations/16973608 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16973608 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16973608 | http://www.w3.org/2000/01/rdf-schema#comment | "Amidoximes can be used as prodrugs for amidines and related functional groups to enhance their intestinal absorption. These prodrugs are reduced to their active amidines. Other N-hydroxylated structures are mutagenic or responsible for toxic effects of drugs and are detoxified by reduction. In this study, a N-reductive enzyme system of pig liver mitochondria using benzamidoxime as a model substrate was identified. A protein fraction free from cytochrome b5 and cytochrome b5 reductase was purified, enhancing 250-fold the minor benzamidoxime-reductase activity catalyzed by the membrane-bound cytochrome b5/NADH cytochrome b5 reductase system. This fraction contained a 35-kDa protein with homologies to the C-terminal domain of the human molybdenum cofactor sulfurase. Here it was demonstrated that this 35-kDa protein contains molybdenum cofactor and forms the hitherto ill defined third component of the N-reductive complex in the outer mitochondrial membrane. Thus, the 35-kDa protein represents a novel group of molybdenum proteins in eukaryotes as it forms the catalytic part of a three-component enzyme complex consisting of separate proteins. Supporting these findings, recombinant C-terminal domain of the human molybdenum cofactor sulfurase exhibited N-reductive activity in vitro, which was strictly dependent on molybdenum cofactor."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m607697200"xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m607697200"xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Clement B."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Clement B."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Bittner F."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Bittner F."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Mendel R."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Mendel R."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Wollers S."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Wollers S."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Havemeyer A."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Havemeyer A."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Kunze T."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/author | "Kunze T."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/pages | "34796-34802"xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/pages | "34796-34802"xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/title | "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."xsd:string |
| http://purl.uniprot.org/citations/16973608 | http://purl.uniprot.org/core/title | "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."xsd:string |