Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco.

@article{Garca1999CharacterizationAS,
  title={Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco.},
  author={Irene Garc{\'i}a and Mark D. Rodgers and R{\'e}gis P{\'e}pin and Ting Fang Hsieh and Michel Matringe},
  journal={Plant physiology},
  year={1999},
  volume={119 4},
  pages={
          1507-16
        }
}
4-Hydroxyphenylpyruvate dioxygenase (4HPPD) catalyzes the formation of homogentisate (2,5-dihydroxyphenylacetate) from p-hydroxyphenylpyruvate and molecular oxygen. In plants this enzyme activity is involved in two distinct metabolic processes, the biosynthesis of prenylquinones and the catabolism of tyrosine. We report here the molecular and biochemical characterization of an Arabidopsis 4HPPD and the compartmentation of the recombinant protein in chlorophyllous tissues. We isolated a 1508-bp… CONTINUE READING
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