Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand binding properties.

@article{Illarionov2001RiboflavinSO,
  title={Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand binding properties.},
  author={Boris Illarionov and Kristina Kemter and Sabine Eberhardt and Gerald Richter and Mark Cushman and Adelbert Bacher},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 15},
  pages={11524-30}
}
Conserved amino acid residues of riboflavin synthase from Escherichia coli were modified by site-directed mutagenesis. Replacement or deletion of phenylalanine 2 afforded catalytically inactive proteins. S41A and H102Q mutants had substantially reduced reaction velocities. Replacements of various other conserved polar residues had little impact on catalytic activity. (19)F NMR protein perturbation experiments using a fluorinated intermediate analog suggest that the N-terminal sequence motif… CONTINUE READING

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