New Knowledge on the Cofactors of Copper Amine Oxidases as a Contribution to Biochemistry of Proteins

Abstract

The review deals with copper/topa quinone-containing oxidases. These enzymes belong to a new protein class of quinoproteins and have been intensively investigated at the present. General properties of the enzymes are surveyed, such as physiological functions of microbial, animal and plant amine oxidases together with the mechanism of the corresponding catalyzed reactions. The major attention is paid to both prosthetic groups of the enzymes - Cu ions and topa quinone bound in the active site. Three-dimensional structures of several amine oxidases obtained by X-ray diffraction analysis of the respective crystals are given in details. Recent results in the biogenesis of quinone cofactor are also presented. The expected ways of further investigation of amine oxidases and some possibilities of their practical application are outlined.