Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase.

@article{Sheu1984StereochemicalCO,
  title={Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase.},
  author={K. F. Sheu and H. Ho and L. Nolan and P. Markovitz and J. Richard and M. F. Utter and P. Frey},
  journal={Biochemistry},
  year={1984},
  volume={23 8},
  pages={
          1779-83
        }
}
  • K. F. Sheu, H. Ho, +4 authors P. Frey
  • Published 1984
  • Chemistry, Computer Science, Medicine
  • Biochemistry
  • Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (Rp)-guanosine 5'-(3-thio[3-18O]triphosphate) and oxalacetate to (Sp)-[18O] thiophosphoenolpyruvate , GDP, and CO2 by a mechanism that involves overall inversion in the configuration of the chiral [18O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [18O]thiophosphoryl group is transferred from (Rp)-guanosine 5'-(3-thio[3-18O]triphosphate) bound at… CONTINUE READING
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