Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.

@article{Murray2001ConservedTI,
  title={Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.},
  author={Jeremy M Murray and Christian R. P. Kurtis and Winston S Tambyrajah and Colin G. Saysell and Carrie M Wilmot and Mark R. Parsons and Simon E V Phillips and Peter Knowles and Michael J McPherson},
  journal={Biochemistry},
  year={2001},
  volume={40 43},
  pages={12808-18}
}
Copper amine oxidases are homodimeric enzymes that catalyze two reactions: first, a self-processing reaction to generate the 2,4,5-trihydroxyphenylalanine (TPQ) cofactor from an active site tyrosine by a single turnover mechanism; second, the oxidative deamination of primary amine substrates with the production of aldehyde, hydrogen peroxide, and ammonia catalyzed by the mature enzyme. The importance of active site residues in both of these processes has been investigated by structural studies… CONTINUE READING