On Carbanion Formation in the Process of Enzymatic Transamination

The rate of decomposition of tetranitromethane in the presence of enzyme‐substrate complexes of l ‐aspartate: 2‐oxoglutarate aminotransferase has been studied; the intermediate Shiff base of aspartate aminotransferase and erythro ‐β‐hydroxy‐ l ‐aspartate was shown to undergo nitration. The catalytic course of nitration of the complex is indicative of predominant modification of the substrate part of the carbanion. The presence of carbanion was demonstrated in the course of both model and enzymatic transamination.