Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis to probe the role of tyrosine 114 in the catalytic mechanism of ADP-glucose synthetase from Escherichia coli.

@article{Kumar1988BiosynthesisOB,
  title={Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis to probe the role of tyrosine 114 in the catalytic mechanism of ADP-glucose synthetase from Escherichia coli.},
  author={Ashir Kumar and Tomoaki Tanaka and Young Mee Lee and Jack Preiss},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 29},
  pages={14634-9}
}
Previous covalent modification studies showed that tyrosine 114 of Escherichia coli ADP-glucose synthetase is involved in substrate binding (Lee, Y. M., and Preiss, J. (1986) J. Biol. Chem. 261, 1058-1064). We have prepared, via site-directed mutagenesis, an E. coli ADP-glucose synthetase variant (Phe114) containing a Tyr114 to Phe substitution in order to test whether the phenolic hydroxyl group plays a critical role in catalysis. Kinetic characterization of Phe114 ADP-glucose synthetase… CONTINUE READING

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