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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/11368174 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11368174 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11368174 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11368174 | http://www.w3.org/2000/01/rdf-schema#comment | "Limonene enantiomers and substrate analogs, including specifically fluorinated derivatives, were utilized to probe active site interactions with recombinant (-)-(4S)-limonene-3-hydroxylase (CYP71D13) and (-)-(4S)-limonene-6-hydroxylase (CYP71D18) from mint (Mentha) species. (-)-(4S)-Limonene is hydroxylated by both enzymes at the designated C3- and C6-allylic positions, with strict regio- and stereospecificity and without detectable allylic rearrangement, to give the corresponding products (-)-trans-isopiperitenol and (-)-trans-carveol. CYP71D13-catalyzed hydroxylation of (+)-(4R)-limonene also yields the corresponding trans-3-hydroxylated product ((+)-transisopiperitenol); however, the C6-hydroxylase converts (+)-(4R)-limonene to a completely different product profile dominated by the enantiopure cis-6-hydroxylated product (+)-cis-carveol along with several minor products, including both enantiomers of the trans-6-hydroxylated product ((+/-)-trans-carveol), indicating allylic rearrangement during catalysis. These results demonstrate that the regiospecificity and facial stereochemistry of oxygen insertion is dictated by the absolute configuration of the substrate. Fluorinated limonene analogs are also tightly bound by both enzymes and hydroxylated at the topologically congruent positions in spite of the polarizing effect of the fluorine atom on substrate reactivity. This strict retention of oxygenation geometry suggests a rigid substrate orientation imposed by multiple hydrophobic active site contacts. Structurally simplified substrate analogs are hydroxylated at slower rates and with substantial loss of regiospecificity, consistent with a loss of active site complementarity. Evaluation of the product profiles generated allowed assessment of the role of hydrophobic contacts in orienting the substrate relative to the activated oxygen species."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.2000.2248"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.2000.2248"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Croteau R."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Croteau R."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Little D.B."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Little D.B."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Schalk M."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Schalk M."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Wuest M."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/author | "Wuest M."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/pages | "125-136"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/pages | "125-136"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/title | "Hydroxylation of limonene enantiomers and analogs by recombinant (-)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/title | "Hydroxylation of limonene enantiomers and analogs by recombinant (-)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites."xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/volume | "387"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://purl.uniprot.org/core/volume | "387"xsd:string |
| http://purl.uniprot.org/citations/11368174 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11368174 |