http://purl.uniprot.org/citations/17395614 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17395614 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17395614 | http://www.w3.org/2000/01/rdf-schema#comment | "Heterotetrameric sarcosine oxidase from Corynebacterium sp.U-96(SO-U96) contains non-covalent and covalent flavins. Lys-358 and Lys-171 in the beta subunit is present at non-covalent flavin adenine dinucleotide (FAD)- and covalent flavin monodinucleotide (FMN)-binding sites, respectively. The Lys-358 mutant, K358R showed 0.07% activity and higher apparent K(m) for sarcosine than the wild-type enzyme, but K358A and K358D mutants showed no activity, suggesting the importance of amino group of Lys358 in the sarcosine-binding to the enzyme. The Lys171 mutants, K171R, K171A and K171D showed 58, 39 and 32% activity of the wild-type enzyme, respectively. An apparent K(m) for oxygen and K(d) of enzyme-sulphite complex increased by the mutation. The rate of reduction of the FAD of K171 mutants with sarcosine did not change by the mutation. The stopped-flow photodiode array analyses of the anaerobic reduction with sarcosin of the wild-type and K171 mutant enzymes showed characteristic spectra of neutral and anionic semiquinones, especially for K171A enzyme. On the basis of these results, the reductive-half reaction of the wild-type and K171 mutant enzymes is explained by a mechanism involving the semiquinones. Low activity of K171 mutants is suggested to be derived from the low rate of oxidation of the reduced FMN in the enzyme."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvm084"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvm084"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Iizuka H."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Iizuka H."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Suzuki H."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Suzuki H."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Saito M."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Saito M."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Kanno M."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/author | "Kanno M."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/pages | "799-815"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/pages | "799-815"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/title | "Kinetic studies on the role of Lys-171 and Lys-358 in the beta subunit of sarcosine oxidase from Corynebacterium sp. U-96."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/title | "Kinetic studies on the role of Lys-171 and Lys-358 in the beta subunit of sarcosine oxidase from Corynebacterium sp. U-96."xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/volume | "141"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://purl.uniprot.org/core/volume | "141"xsd:string |
http://purl.uniprot.org/citations/17395614 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17395614 |
http://purl.uniprot.org/citations/17395614 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17395614 |