Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.

@article{Chen2000CrystalSA,
  title={Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.},
  author={Zuxiong Chen and Benjamin K Schwartz and Neal K. Williams and Rong Xun Li and Judith P Klinman and F. Schuyler Mathews},
  journal={Biochemistry},
  year={2000},
  volume={39 32},
  pages={
          9709-17
        }
}
Copper amine oxidases (CAOs) catalyze the two-electron oxidation of primary amines to aldehydes, utilizing molecular oxygen as a terminal electron acceptor. To accomplish this transformation, CAOs utilize two cofactors: a mononuclear copper, and a unique redox cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ or TOPA quinone). TPQ is derived via posttranslational modification of a specific tyrosine residue within the protein itself. In this study, the structure of an amine oxidase from… CONTINUE READING
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