| http://purl.uniprot.org/citations/10655615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10655615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10655615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/10655615 | http://www.w3.org/2000/01/rdf-schema#comment | "Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine beta-lactamases. The first CAS-catalyzed step (hydroxylation) is separated from the latter two (oxidative cyclization/desaturation) by the action of an amidinohydrolase. Here, we describe crystal structures of CAS in complex with Fe(II), 2-oxoglutarate (2OG) and substrates (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS catalyzes formation of the clavam nucleus, via a process unprecedented in synthetic organic chemistry, and suggest how it discriminates between substrates and controls reaction of its highly reactive ferryl intermediate. The presence of an unpredicted jelly roll beta-barrel core in CAS implies divergent evolution within the family of 2OG and related oxygenases. Comparison with other non-heme oxidases/oxygenases reveals flexibility in the position which dioxygen ligates to the iron, in contrast to the analogous heme-using enzymes."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.org/dc/terms/identifier | "doi:10.1038/72398"xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.org/dc/terms/identifier | "doi:10.1038/72398"xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Zhang Z."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Ren J.-S."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Ren J.-S."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Harlos K."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Harlos K."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Stammers D.K."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Stammers D.K."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Baldwin J.E."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/author | "Baldwin J.E."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/pages | "127-133"xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/pages | "127-133"xsd:string |
| http://purl.uniprot.org/citations/10655615 | http://purl.uniprot.org/core/title | "Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase."xsd:string |