Plant Physiol. Drug Metab Dispos
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PLANT PHYSIOLOGY , Vol 101, Issue 3 925-930, Copyright © 1993 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Characterization and Solubilization of Kaurenoic Acid Hydroxylase from Gibberella fujikuroi

J. C. Jennings, R. C. Coolbaugh, D. A. Nakata and C. A. West
Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907 (J.C.J., R.C.C.)

A key step in gibberellin biosynthesis is the conversion of ent-kaurenoic acid to ent-7[alpha]-hydroxykaurenoic acid, mediated by the enzyme kaurenoic acid hydroxylase. A cell-free system obtained from Gibberella fujikuroi (Saw.) Wr. was used to characterize kaurenoic acid hydroxylase activity. Microsomal preparations from disrupted fungal cells, in the presence of O2 and NADPH, converted [17-14C]ent-kaurenoic acid to oxidation products that were separated by high-performance liquid chromatography and identified as ent-7[alpha]-hydroxykaurenoic acid and gibberellin A14 by combined gas chromatography-mass spectrometry. Flavin adenine dinucleotide and the chloride salts of several monovalent cations stimulated the conversion of ent-kaurenoic acid to these products, whereas CO and a number of known inhibitors of cytochrome P-450-dependent reactions, including paclobutrazol, tetcyclacis, BAS 111..W, flurprimidol, triarimol, metyrapone, and 1-phenylimida-zole, significantly reduced kaurenoic acid hydroxylase activity. Kaurenoic acid hydroxylase was solubilized from fungal microsomes by treatment with 1 M KCl. The properties of the enzyme noted above suggest that kaurenoic acid hydroxylase from G. fujikuroi is a cytochrome P-450-dependent monooxygenase.


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Copyright © 1993 by the American Society of Plant Biologists