BIOTIN ACTIVATION OF CERTAIN DEAMINASES

Abstract

In a previous paper' we have demonstrated that biotin is involved in the decarboxylation of oxalacetate.It has now been found that the deaminases for aspartic acid, serine, and threonine may be resolved by the same techniques used previously (exposure of the living bacterial cells to M phosphate at pH 4 for 30 minutes at 27-37"), and that the lost activity is restored specifically by biotin.The data !n the table indicate that a mixture of vitamins lacking in biotin has little or no effect, while the same mixture with added biotin effectively activates the resolved enzymes.Biotin alone is virtually as active as the vitamin mixture.The reversal of the aspartic deaminase shows a similar response to biotin.These results demonstrate a second r81e for biotin which may help to explain the results of previous investigators.2(See following page.for the table.)