| http://purl.uniprot.org/citations/16492736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16492736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16492736 | http://www.w3.org/2000/01/rdf-schema#comment | "Lutein, a dihydroxy derivative of alpha-carotene (beta,epsilon-carotene), is the most abundant carotenoid in photosynthetic plant tissues where it plays important roles in light-harvesting complex-II structure and function. The synthesis of lutein from lycopene requires at least four distinct enzymatic reactions: beta- and epsilon-ring cyclizations and hydroxylation of each ring at the C-3 position. Three carotenoid hydroxylases have already been identified in Arabidopsis, two nonheme diiron beta-ring monooxygenases (the B1 and B2 loci) that primarily catalyze hydroxylation of the beta-ring of beta,beta-carotenoids and one heme-containing monooxygenase (CYP97C1, the LUT1 locus) that catalyzes hydroxylation of the epsilon-ring of beta,epsilon-carotenoids. In this study, we demonstrate that Arabidopsis CYP97A3 (the LUT5 locus) encodes a fourth carotenoid hydroxylase with major in vivo activity toward the beta-ring of alpha-carotene (beta,epsilon-carotene) and minor activity on the beta-rings of beta-carotene (beta,beta-carotene). A cyp97a3-null allele, lut5-1, causes an accumulation of alpha-carotene at a level equivalent to beta-carotene in wild type, which is stably incorporated into photosystems, and a 35% reduction in beta-carotene-derived xanthophylls. That lut5-1 still produces 80% of wild-type lutein levels, indicating at least one of the other carotene hydroxylases, can partially compensate for the loss of CYP97A3 activity. From these data, we propose a model for the preferred pathway for lutein synthesis in plants: ring cyclizations to form alpha-carotene, beta-ring hydroxylation of alpha-carotene by CYP97A3 to produce zeinoxanthin, followed by epsilon-ring hydroxylation of zeinoxanthin by CYP97C1 to produce lutein."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0511207103"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0511207103"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/author | "Kim J."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/author | "Kim J."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/author | "DellaPenna D."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/author | "DellaPenna D."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/pages | "3474-3479"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/pages | "3474-3479"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/title | "Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/title | "Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3."xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/volume | "103"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://purl.uniprot.org/core/volume | "103"xsd:string |
| http://purl.uniprot.org/citations/16492736 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16492736 |
| http://purl.uniprot.org/citations/16492736 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16492736 |
| http://purl.uniprot.org/citations/16492736 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16492736 |
| http://purl.uniprot.org/citations/16492736 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16492736 |
| http://purl.uniprot.org/uniprot/Q93VK5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16492736 |
| http://purl.uniprot.org/uniprot/Q93VK5#attribution-1113D91877F7D5A6C2E84772A283460D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/16492736 |