Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.

@article{Ishii1996FunctionallyIR,
  title={Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.},
  author={Seiji Ishii and Hiroyuki Mizuguchi and Junichi Nishino and Hideyuki Hayashi and Hiroyuki Kagamiyama},
  journal={Journal of biochemistry},
  year={1996},
  volume={120 2},
  pages={369-76}
}
To identify functional residues of rat liver L-aromatic amino acid decarboxylase (AADC), we aligned the sequences of 13 group II amino acid decarboxylases and performed mutational analysis on the residues that were invariant or conservatively substituted. Replacements of His192, Asp252, Asp271, Ser296, Lys303, Tyr332, and Arg355 with alanine residues decreased the AADC activity (kcat/K(m)) by more than 10(4)-fold. Conservative replacements of [Asp252-->Glu], [Lys303-->Arg], and [Tyr332-->Phe… CONTINUE READING