Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase.

@article{Inglese1990SubcloningCA,
  title={Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase.},
  author={J Inglese and Dana L. Johnson and A L Shiau and Joseph A. M. Smith and Stephen J Benkovic},
  journal={Biochemistry},
  year={1990},
  volume={29 6},
  pages={1436-43}
}
Glycinamide ribonucleotide transformylase (GAR TFase; EC 2.1.2.2) has been purified 70-fold to apparent homogeneity from Escherichia coli harboring an expression vector encoding the purN gene product, GAR TFase. The protein is a monomer of Mr 23,241 and catalyzes a single reaction. Steady-state kinetic parameters for the enzyme have been obtained. The structural requirements for cofactor utilization have been investigated and found to parallel those of the multifunctional avian enzyme. The… CONTINUE READING

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