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http://purl.uniprot.org/citations/20675294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20675294http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20675294http://www.w3.org/2000/01/rdf-schema#comment"We characterized the crystal structures of heterotetrameric sarcosine oxidase (SO) from Corynebacterium sp. U-96 complexed with methylthioacetate (MTA), pyrrole 2-carboxylate (PCA) and sulphite, and of sarcosine-reduced SO. SO comprises α-, β-, γ- and δ-subunits; FAD and FMN cofactors; and a large internal cavity. MTA and PCA are sandwiched between the re-face of the FAD isoalloxazine ring and the β-subunit C-terminal residues. Reduction of flavin cofactors shifts the β-subunit Ala1 towards the α-subunit Met55, forming a surface cavity at the oxygen-channel vestibule and rendering the β-subunit C-terminal residues mobile. We identified three channels connecting the cavity and the enzyme surface. Two of them exist in the inter-subunit space between α and β-subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the re-side of the FAD isoalloxazine ring by traversing the mobile β-subunit C-terminal residues. The third channel goes through the α-subunit and has a folinic acid-binding site, where the iminium intermediate is converted to Gly and either formaldehyde or, 5,10-methylenetetrahydrofolate. Oxygen molecules are probably located on the surface cavity and diffuse to the FMN isoalloxazine ring; the H(2)O(2) formed exits via the oxygen channel."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvq083"xsd:string
http://purl.uniprot.org/citations/20675294http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvq083"xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Moriguchi T."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Moriguchi T."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Ueno G."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Ueno G."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Ida K."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Ida K."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Hikima T."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/author"Hikima T."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/pages"491-505"xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/pages"491-505"xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/title"Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96."xsd:string
http://purl.uniprot.org/citations/20675294http://purl.uniprot.org/core/title"Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96."xsd:string