ABA 9'-hydroxylation is catalyzed by CYP707A in Arabidopsis

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DOIResolve DOI: http://doi.org/10.1016/j.phytochem.2011.02.004
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TypeArticle
Journal titlePhytochemistry
Volume72
Issue8
Pages717722; # of pages: 6
SubjectArabidopsis; abscisic acid; catabolism; P450; CYP707A; neophaseic acid; phaseic acid
AbstractAbscisic acid (ABA) catabolism is important for regulating endogenous ABA levels. Neophaseic acid (neoPA) is one of the ABA catabolites produced via ABA 9'-hydroxylation, but the gene encoding ABA 9'-hydroxylase has not been identified. We found that endogenous neoPA levels reduced in loss-of-function mutants defective in ABA 8'-hydroxylase (CYP707A) genes. In addition, levels of both neoPA and PA reduced similarly when wild-type plants were treated with uniconazole-P, a P450 inhibitor. Furthermore, in vitro enzyme assay using microsomal fraction from yeast expressing CYP707A showed that all four Arabidopsis CYP707As contained both ABA 8'- and 9'-hydroxylase activities, although ABA 9'-hydroxylase activity is minor. These results demonstrate that ABA 9'- hydroxylation is catalyzed by CYP707A as a side reaction in Arabidopsis.
Publication date
LanguageEnglish
AffiliationNRC Plant Biotechnology Institute; National Research Council Canada
Peer reviewedYes
NRC number50177
NPARC number18856993
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Record identifier6fe8d976-cdf5-4451-b340-d0da5001aaaa
Record created2012-03-30
Record modified2016-05-09
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