Isolation of herbicide-resistant 4-hydroxyphenylpyruvate dioxygenase from cultured Coptis japonica cells.
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.
Liang
Yuling
Y
State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, PR China.
Minami
Hiromichi
H
Sato
Fumihiko
F
D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001599:Berberine / Q000378:metabolism; D002478:Cells, Cultured; D039323:Coptis / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D015723:Gene Library; D053209:Herbicide Resistance; D006540:Herbicides / Q000494:pharmacology*; D006801:Humans; D008969:Molecular Sequence Data; D011720:Pyrazoles / Q000494:pharmacology
D006540:Herbicides; D011720:Pyrazoles; C534728:destosyl pyrazolate; D001599:Berberine; D015111:4-Hydroxyphenylpyruvate Dioxygenase