Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida.

@article{Rther2001CharacterizationOT,
  title={Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida.},
  author={Dagmar R{\"o}ther and L{\'a}szl{\'o} Poppe and Sandra Viergutz and Birgid Langer and J{\'a}nos R{\'e}tey},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 23},
  pages={6011-9}
}
Elucidation of the 3D structure of histidine ammonia-lyase (HAL, EC 4.3.1.3) from Pseudomonas putida by X-ray crystallography revealed that the electrophilic prosthetic group at the active site is 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) [Schwede, T.F., Rétey, J., Schulz, G.E. (1999) Biochemistry, 38, 5355-5361]. To evaluate the importance of several amino-acid residues at the active site for substrate binding and catalysis, we mutated the following amino-acid codons in the HAL gene… CONTINUE READING