Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2006-3-15
pubmed:databankReference
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-10338008, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-10536025, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-11127994, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-11587509, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-11997140, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-12351216, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-12618384, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-12712234, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-12782726, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-14563924, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-14676196, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-14709673, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-14717605, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-14727092, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-15029188, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-15325908, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-15709776, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-15723551, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-3109324, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-3924614, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-7724673, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-8068688, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-8578971, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-8798688, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-8837512, http://linkedlifedata.com/resource/pubmed/commentcorrection/16492736-8837513
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3474-9
pubmed:dateRevised
2010-9-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't