Abstract
4-Hydroxyphenylpyruvate dioxygenase (HPPD) catalyzes the formation of homogentisate from 4-hydroxyphenylpyruvate and O(2). In plants, HPPD has been identified as a molecular target for herbicides. We report the isolation and characterization of a cDNA encoding a HPPD from cultured Coptis japonica cells. Recombinant CjHPPD showed significantly higher half-maximum inhibitory concentration (IC(50)) values for the HPPD-inhibiting herbicide destosyl pyrazolate than other plant HPPDs.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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4-Hydroxyphenylpyruvate Dioxygenase / antagonists & inhibitors
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4-Hydroxyphenylpyruvate Dioxygenase / genetics
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4-Hydroxyphenylpyruvate Dioxygenase / isolation & purification*
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4-Hydroxyphenylpyruvate Dioxygenase / metabolism*
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Amino Acid Sequence
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Berberine / metabolism
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Cells, Cultured
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Coptis / cytology*
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Coptis / drug effects
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Coptis / enzymology*
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Coptis / metabolism
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Gene Library
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Herbicide Resistance
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Herbicides / pharmacology*
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Humans
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Molecular Sequence Data
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Pyrazoles / pharmacology
Substances
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Herbicides
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Pyrazoles
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destosyl pyrazolate
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Berberine
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4-Hydroxyphenylpyruvate Dioxygenase