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.