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- W1606843108 endingPage "1299" @default.
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- W1606843108 abstract "Abstract Amine oxidases (EC 1.4.3.6) that contain copper/topa quinone cofactor belong to a new protein group of quinoproteins emerging in recent years. This review brings together information on the general properties of the enzymes and their Physiol.ogical functions. In plants, theseenzymes are involved in processes of development and senescence, they reduce the concentration of toxic amines produced during exposure to stress conditions, provide hydrogen peroxide for wall stiffening and lignification and precursor compounds for biosynthesis of some alkaloids. Majorattention is currently being paid to the structure of the active site of the enzymes that contains copper ions and a posttranslationally modified tyrosyl residue, topa quinone. Three-dimensional structures recently obtained for several amine oxidases by X-ray diffraction analysis of the respective crystals provide important structural information about the unique protein folding of the native enzyme and Mol.ecular arrangement of the active site. Biogenesis of the quinone cofactor is another issue that is addressed frequently at present. Differences between copper/topa quinone-containing amine oxidases and flavoprotein polyamine oxidases are outlined. Finally, future research directions on amine oxidases and the possibilities of their practical application are discussed." @default.
- W1606843108 created "2016-06-24" @default.
- W1606843108 creator A5000518502 @default.
- W1606843108 creator A5050518858 @default.
- W1606843108 creator A5051710329 @default.
- W1606843108 creator A5076596907 @default.
- W1606843108 date "2002-01-01" @default.
- W1606843108 modified "2023-09-27" @default.
- W1606843108 title "Copper/topa quinone-containing amine oxidases — Recent research developments" @default.
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