Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase.

@article{Mure2005RoleOT,
  title={Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase.},
  author={M. Garcia del Mure and Doreen E. Brown and Colin G. Saysell and Melanie S. Rogers and Carrie M Wilmot and Christian R. P. Kurtis and Michael J McPherson and Simon E V Phillips and Peter Knowles and David M. Dooley},
  journal={Biochemistry},
  year={2005},
  volume={44 5},
  pages={
          1568-82
        }
}
2-Hydrazinopyridine (2HP) is an irreversible inhibitor of copper amine oxidases (CAOs). 2HP reacts directly at the C5 position of the TPQ cofactor, yielding an intense chromophore with lambda(max) approximately 430 nm (adduct I) in Escherichia coli amine oxidase (ECAO). The adduct I form of wild type (WT-ECAO) was assigned as a hydrazone on the basis of the X-ray crystal structure. The hydrazone adduct appears to be stabilized by two key hydrogen-bonding interactions between the TPQ-2HP moiety… CONTINUE READING
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