In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene.

@article{Pitterle1993InVS,
  title={In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene.},
  author={Diana M Pitterle and Jean Luc Johnson and Krishnakumar Rajagopalan},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 18},
  pages={
          13506-9
        }
}
The pterin component of the molybdenum cofactor, termed molybdopterin, is synthesized in Escherichia coli by enzymes encoded at the chl loci. A late step in the biosynthetic pathway, the conversion of a molybdopterin intermediate, precursor Z, to molybdopterin, requires the activity of a two-subunit protein, the converting factor. Precursor Z has many of the features of molybdopterin but lacks the dithiolene function essential for molybdenum ligation. Conversion of precursor Z to molybdopterin… CONTINUE READING

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