| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/2000/01/rdf-schema#comment | "Penicillin antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the beta-lactam and thiazolidine rings of the nucleus are created, is mediated by isopenicillin N synthase (IPNS), which binds ferrous iron and uses dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical precedent, IPNS catalyses the transfer of four hydrogen atoms from its tripeptide substrate to dioxygen forming, in a single reaction, the complete bicyclic nucleus of the penicillins. We now report the structure of IPNS complexed with manganese, which reveals the active site is unusually buried within a 'jelly-roll' motif and lined by hydrophobic residues, and suggest how this structure permits the process of penicillin formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.org/dc/terms/identifier | "doi:10.1038/375700a0"xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.org/dc/terms/identifier | "doi:10.1038/375700a0"xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7791906 |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7791906 |
| http://purl.uniprot.org/citations/7791906 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7791906 |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Andersson I."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Andersson I."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Harlos K."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Harlos K."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Barton G.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Barton G.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Clifton I.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Clifton I.J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Fueloep V."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Fueloep V."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Hajdu J."xsd:string |
| http://purl.uniprot.org/citations/7791906 | http://purl.uniprot.org/core/author | "Hajdu J."xsd:string |