The Enzyme System of Trans-Animation, its Mode of Action and Biological Significance

Abstract

THE reversible transfer of amino groups between aminodicarboxylic acids and α-ketoacids, or ‘trans-amination’, reported in a series of papers by me and my associates1, is of almost universal occurrence in biological objects. It is readily effected by most animal tissues2, and also, as shown in this laboratory and independently by Virtanen3 and Euler et al.4, by vegetable tissues and micro-organisms. Trans-amination is effected by a special group of intracellular enzymes, for which the name amino-pherases is suggested (in preference to the clumsy although more precise term aminotransportases). As trans-amination involves intermolecular oxido-reduction, the aminopherases should be classed among the desmolases. They differ in mode of action and in many properties from the formerly known enzymes of amino acid metabolism, including the I- and d-deaminases and specific glutamic and aspartic dehydrogenases.