Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol.

@article{Rohdich1999Cytidine5B,
  title={Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol.},
  author={Felix Rohdich and Juraithip Wungsintaweekul and Monika Fellermeier and Silvia Sagner and Stefan Herz and Klaus Kis and Wolfgang Eisenreich and Adelbert Bacher and Meinhart H. Zenk},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 21},
  pages={
          11758-63
        }
}
2-C-methylerythritol 4-phosphate has been established recently as an intermediate of the deoxyxylulose phosphate pathway used for biosynthesis of terpenoids in plants and in many microorganisms. We show that an enzyme isolated from cell extract of Escherichia coli converts 2-C-methylerythritol 4-phosphate into 4-diphosphocytidyl-2-C-methylerythritol by reaction with CTP. The enzyme is specified by the hitherto unannotated ORF ygbP of E. coli. The cognate protein was obtained in pure form from a… CONTINUE READING

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