| http://purl.uniprot.org/citations/19490124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19490124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19490124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/19490124 | http://www.w3.org/2000/01/rdf-schema#comment | "The nonheme iron oxygenase VioC from Streptomyces vinaceus catalyzes Fe(II)-dependent and alpha-ketoglutarate-dependent Cbeta-hydroxylation of L-arginine during the biosynthesis of the tuberactinomycin antibiotic viomycin. Crystal structures of VioC were determined in complexes with the cofactor Fe(II), the substrate L-arginine, the product (2S,3S)-hydroxyarginine and the coproduct succinate at 1.1-1.3 A resolution. The overall structure reveals a beta-helix core fold with two additional helical subdomains that are common to nonheme iron oxygenases of the clavaminic acid synthase-like superfamily. In contrast to other clavaminic acid synthase-like oxygenases, which catalyze the formation of threo diastereomers, VioC produces the erythro diastereomer of Cbeta-hydroxylated L-arginine. This unexpected stereospecificity is caused by conformational control of the bound substrate, which enforces a gauche(-) conformer for chi(1) instead of the trans conformers observed for the asparagine oxygenase AsnO and other members of the clavaminic acid synthase-like superfamily. Additionally, the substrate specificity of VioC was investigated. The side chain of the L-arginine substrate projects outwards from the active site by undergoing interactions mainly with the C-terminal helical subdomain. Accordingly, VioC exerts broadened substrate specificity by accepting the analogs L-homoarginine and L-canavanine for Cbeta-hydroxylation."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1742-4658.2009.07085.x"xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1742-4658.2009.07085.x"xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Marahiel M.A."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Marahiel M.A."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Essen L.O."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Essen L.O."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Helmetag V."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Helmetag V."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Samel S.A."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Samel S.A."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Thomas M.G."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/author | "Thomas M.G."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/pages | "3669-3682"xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/pages | "3669-3682"xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/title | "Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/title | "Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/19490124 | http://purl.uniprot.org/core/volume | "276"xsd:string |