Abstract
Cytochrome P450-dependent monooxygenases are a large group of heme-containing enzymes, most of which catalyze NADPH- and O2-dependent hydroxylation reactions. The cloning of plant P450s has been hampered because these membrane-localized proteins are typically present in low abundance and are often unstable to purification. Since the cloning of the first plant P450 gene in 1990, there has been an explosion in the rate at which genes encoding plant P450s have been identified. These successes have largely been the result of advances in purification techniques, as well as the application of alternative methods such as mutant- and PCR-based cloning strategies. The availability of these cloned genes has made possible the analysis of P450 gene regulation and may soon reveal aspects of the evolution of P450s in plants. This new knowledge will significantly improve our understanding of many metabolic pathways and may permit their manipulation in the near future.
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