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We have reported previously that biotin, as well as muscle adenylic acid, is somehow concerned in the reversible deamination of aspartic acid, and in the deamination of serine and threonine (Lichstein and Umbreit, 1947a; Lichstein and Christman, 1948). This has been demonstrated by employing an aging technique consisting of the exposure of living bacterial cell suspensions to molar phosphate at pH 4 for a short time (Lichstein and Umbreit, 1947a,b; Lichstein and Christman, 1948). The intimate relationship of biotin and adenylic acid to aspartic acid deaminase has been extended to partially resolved cell-free preparations. It has been shown also that yeast extract is approximately 100-fold more active in the stimulation of partially resolved aspartic acid deaminase than could be accounted for by its assayable biotin content. Studies with such preparations suggested that the preformed coenzyme of aspartic acid deaminase exists in yeast extract and that both biotin and adenylic acid are somehow concerned in its formation (Lichstein, 1949).

THE NATURE OF THE COENZYME OF ASPARTIC ACID, SERINE, AND THREONINE DEAMINASES