Uncovering the determinants of a highly perturbed tyrosine pKa in the active site of ketosteroid isomerase.

@article{Schwans2013UncoveringTD,
  title={Uncovering the determinants of a highly perturbed tyrosine pKa in the active site of ketosteroid isomerase.},
  author={Jason P Schwans and Fanny Sunden and Ana Gonz{\'a}lez and Yingssu Tsai and Daniel Herschlag},
  journal={Biochemistry},
  year={2013},
  volume={52 44},
  pages={
          7840-55
        }
}
Within the idiosyncratic enzyme active-site environment, side chain and ligand pKa values can be profoundly perturbed relative to their values in aqueous solution. Whereas structural inspection of systems has often attributed perturbed pKa values to dominant contributions from placement near charged groups or within hydrophobic pockets, Tyr57 of a Pseudomonas putida ketosteroid isomerase (KSI) mutant, suggested to have a pKa perturbed by nearly 4 units to 6.3, is situated within a solvent… CONTINUE READING
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