Evolution of vitamin B2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin.

@article{Fischer2004EvolutionOV,
  title={Evolution of vitamin B2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin.},
  author={Markus Fischer and Werner R{\"o}misch and Sabine Saller and Boris Illarionov and Gerald Richter and Felix Rohdich and Wolfgang Eisenreich and Adelbert Bacher},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 35},
  pages={36299-308}
}
The Arabidopsis thaliana open reading frame At4g20960 predicts a protein whose N-terminal part is similar to the eubacterial 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate deaminase domain. A synthetic open reading frame specifying a pseudomature form of the plant enzyme directed the synthesis of a recombinant protein which was purified to apparent homogeneity and was shown by NMR spectroscopy to convert 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6… CONTINUE READING
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