Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase.

@article{Bertoldi2002MutationOT,
  title={Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase.},
  author={Mariarita Bertoldi and Marco Gonsalvi and Roberto Contestabile and Carla Borri Voltattorni},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 39},
  pages={36357-62}
}
A flexible loop (residues 328-339), presumably covering the active site upon substrate binding, has been revealed in 3,4-dihydroxyphenylalanine decarboxylase by means of kinetic and structural studies. The function of tyrosine 332 has been investigated by substituting it with phenylalanine. Y332F displays coenzyme content and spectroscopic features identical to those of the wild type. Unlike wild type, during reactions with l-aromatic amino acids under both aerobic and anaerobic conditions… CONTINUE READING

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