| Abstract: | Enzymic memory is a kinetic phenomenon observable in double displacement mechanisms. The defining feature of enzymic memory is the occurrence of different rates of transfer for a common transferable group from the substituted enzymes obtained with different donor substrates. Memory behavior was previously demonstrated for both the bovine and human liver rhodaneses (EC 2.8.1.1). Steady state kinetic tests for enzymic memory have now been done with ascorbate oxidase (EC 1.10.3.3) and aspartate aminotransferase (EC 2.6.1.1). The results were positive with ascorbate oxidase, which showed an oxygen reactivity ratio of 1:20:300 for the reduced enzymes obtained with reductate, araboascorbate, and ascorbate, respectively. Results were negative for the aminotransferase tested with the alternate donors glutamate and cysteine sulfinate, with oxaloacetate as the common acceptor. The structural basis of the ascorbate oxidase results was probed by comparison of both the ultraviolet absorption and fluorescence spectra of the oxidized enzyme with those of the reduced forms obtained with ascorbate and reductate. The results are consistent with a conformational basis for the memory phenomenon. |
