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The CYP701B1 of Physcomitrella patens is an ent ‐kaurene oxidase that resists inhibition by uniconazole‐P
Author(s) -
Miyazaki Sho,
Katsumata Takumi,
Natsume Masahiro,
Kawaide Hiroshi
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.057
Subject(s) - physcomitrella patens , oxidase test , biochemistry , yeast , biosynthesis , arabidopsis thaliana , arabidopsis , gene , enzyme , biology , gibberellin , chemistry , mutant , botany
The moss Physcomitrella patens produces both ent ‐kaurene and ent ‐kaurenoic acid, which are intermediates of gibberellin biosynthesis in flowering plants. The CYP701 superfamily of cytochrome P450s functions as ent ‐kaurene oxidases in the biosynthesis of ent ‐kaurenoic acid. A candidate gene encoding ent ‐kaurene oxidase in P. patens , CYP701B1 , was cloned and heterologously expressed in yeast to examine enzyme activities in vitro. The recombinant CYP701B1 protein catalyzed the oxidation reaction from ent ‐kaurene to ent ‐kaurenoic acid. CYP701B1 activity was highly resistant to the ent ‐kaurene oxidase inhibitor uniconazole‐P (IC 50 64 μM), even though the activity of Arabidopsis ent‐ kaurene oxidase (CYP701A3) was sensitive (IC 50 0.26 μM).