Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy.

@article{Sura2006EffectsOL,
  title={Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy.},
  author={Giri R Sura and Mauricio D Lasagna and Vijay B. Gawandi and Gregory D. Reinhart and Paul F Fitzpatrick},
  journal={Biochemistry},
  year={2006},
  volume={45 31},
  pages={
          9632-8
        }
}
Fluorescence anisotropy has been used to monitor the effect of ligands on a mobile loop over the active site of tyrosine hydroxylase. Phe184 in the center of the loop was mutated to tryptophan, and the three native tryptophan residues were mutated to phenylalanine to form an enzyme with a single tryptophan residue in the mobile loop. The addition of 6-methyl-5-deazatetrahydropterin to the enzyme resulted in a significant increase in the fluorescence anisotropy. The addition of phenylalanine did… CONTINUE READING

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