| http://purl.uniprot.org/citations/23844678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23844678 | http://www.w3.org/2000/01/rdf-schema#comment | "The crystal structure of 2-methylisoborneol synthase (MIBS) from Streptomyces coelicolor A3(2) has been determined in its unliganded state and in complex with two Mg(2+) ions and 2-fluoroneryl diphosphate at 1.85 and 2.00 Å resolution, respectively. Under normal circumstances, MIBS catalyzes the cyclization of the naturally occurring, noncanonical 11-carbon isoprenoid substrate, 2-methylgeranyl diphosphate, which first undergoes an ionization-isomerization-ionization sequence through the tertiary diphosphate intermediate 2-methyllinalyl diphosphate to enable subsequent cyclization chemistry. MIBS does not exhibit catalytic activity with 2-fluorogeranyl diphosphate, and we recently reported the crystal structure of MIBS complexed with this unreactive substrate analogue [ Köksal, M., Chou, W. K. W., Cane, D. E., Christianson, D. W. (2012) Biochemistry 51 , 3011-3020 ]. However, cocrystallization of MIBS with the fluorinated analogue of the tertiary allylic diphosphate intermediate, 2-fluorolinalyl diphosphate, reveals unexpected reactivity for the intermediate analogue and yields the crystal structure of the complex with the primary allylic diphosphate, 2-fluoroneryl diphosphate. Comparison with the structure of the unliganded enzyme reveals that the crystalline enzyme active site remains partially open, presumably due to the binding of only two Mg(2+) ions. Assays in solution indicate that MIBS catalyzes the generation of (1R)-(+)-camphor from the substrate 2-fluorolinalyl diphosphate, suggesting that both 2-fluorolinalyl diphosphate and 2-methyllinalyl diphosphate follow the identical cyclization mechanism leading to 2-substituted isoborneol products; however, the initially generated 2-fluoroisoborneol cyclization product is unstable and undergoes elimination of hydrogen fluoride to yield (1R)-(+)-camphor."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400797c"xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/author | "Christianson D.W."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/author | "Chou W.K."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/author | "Cane D.E."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/author | "Koksal M."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/pages | "5247-5255"xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/title | "Unexpected reactivity of 2-fluorolinalyl diphosphate in the active site of crystalline 2-methylisoborneol synthase."xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://purl.uniprot.org/core/volume | "52"xsd:string |
| http://purl.uniprot.org/citations/23844678 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23844678 |
| http://purl.uniprot.org/citations/23844678 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23844678 |
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| http://purl.uniprot.org/uniprot/Q9F1Y6 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23844678 |