Characterization and functional identification of a novel plant 4,5-extradiol dioxygenase involved in betalain pigment biosynthesis in Portulaca grandiflora.

@article{Christinet2004CharacterizationAF,
  title={Characterization and functional identification of a novel plant 4,5-extradiol dioxygenase involved in betalain pigment biosynthesis in Portulaca grandiflora.},
  author={Laurent Christinet and Fr{\'e}d{\'e}ric X. Burdet and Ma{\"i}a Zaiko and Ursula Hinz and Jean-Pierre Zr{\"y}d},
  journal={Plant physiology},
  year={2004},
  volume={134 1},
  pages={265-74}
}
Betalains are pigments that replace anthocyanins in the majority of families of the plant order Caryophyllales. Betalamic acid is the common chromophore of betalains. The key enzyme of the betalain biosynthetic pathway is an extradiol dioxygenase that opens the cyclic ring of dihydroxy-phenylalanine (DOPA) between carbons 4 and 5, thus producing an unstable seco-DOPA that rearranges nonenzymatically to betalamic acid. A gene for a 4,5-DOPA-dioxygenase has already been isolated from the fungus… CONTINUE READING
Highly Influential
This paper has highly influenced 11 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 35 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 39 references

Cloning and expression of a cDNA encoding betanidin 5O - glucosyltransferase , a betanidin - and flavonoid - specific enzyme with high homology to inducible glucosyltransferases from the Solanaceae

  • K Yamamoto, N Kobayashi, K Yoshitama, S Teramoto, A Komamine
  • Plant J
  • 1999

Similar Papers

Loading similar papers…