Copper amine oxidase: a novel use for a tyrosine.
The first three-dimensional structure of copper amine oxidase demonstrates that one tyrosine residue is converted into 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ binds to copper in the inactive form of the enzyme but not in the active form.
Fontecave
M
M
Laboratoire d'Etudes Dynamiques et Structurales de la Sélectivité, URA CNRS 332, Université Joseph Fourier, Grenoble, France.
Eklund
H
H
D006631:Amine Oxidase (Copper-Containing) / Q000037:antagonists & inhibitors / Q000737:chemistry*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry*; D001665:Binding Sites; D002384:Catalysis; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011487:Protein Conformation; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D014443:Tyrosine / Q000737:chemistry*
C086758:2,4,5-trihydroxyphenylalanine quinone; D001426:Bacterial Proteins; D000644:Quaternary Ammonium Compounds; D014443:Tyrosine; D004295:Dihydroxyphenylalanine; D006631:Amine Oxidase (Copper-Containing)