The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor.

@article{Pitterle1993TheBO,
  title={The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor.},
  author={Diana M. Pitterle and K. V. Rajagopalan},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 18},
  pages={
          13499-505
        }
}
Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Active converting factor has been purified from Escherichia coli chlA1 cells and found to have two subunits of mass 10 and 16 kDa. Electrophoresis of the purified converting factor on denaturing polyacrylamide gels revealed the presence of a 27-kDa protein as well… CONTINUE READING

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