Folate synthesis in plants: the last step of the p-aminobenzoate branch is catalyzed by a plastidial aminodeoxychorismate lyase.

@article{Basset2004FolateSI,
  title={Folate synthesis in plants: the last step of the p-aminobenzoate branch is catalyzed by a plastidial aminodeoxychorismate lyase.},
  author={Gilles J. C. Basset and St{\'e}phane Ravanel and Eoin P. Quinlivan and Ruth White and James J. Giovannoni and Fabrice R{\'e}beill{\'e} and Brian P Nichols and Kazuo Shinozaki and Motoaki Seki and J. Gregory and Andrew D. Hanson},
  journal={The Plant journal : for cell and molecular biology},
  year={2004},
  volume={40 4},
  pages={453-61}
}
In plants, the last step in the synthesis of p-aminobenzoate (PABA) moiety of folate remains to be elucidated. In Escherichia coli, this step is catalyzed by the PabC protein, a beta-lyase that converts 4-amino-4-deoxychorismate (ADC)--the reaction product of the PabA and PabB enzymes--to PABA and pyruvate. So far, the only known plant enzyme involved in PABA synthesis is ADC synthase, which has fused domains homologous to E. coli PabA and PabB and is located in plastids. ADC synthase has no… CONTINUE READING
14 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Similar Papers

Loading similar papers…