Abstract
Twarog, R. (University of Illinois, Urbana) and R. S. Wolfe. Role of butyryl phosphate in the energy metabolism of Clostridium tetanomorphum. J. Bacteriol. 86:112-117. 1963.-A partially purified butyrokinase from Clostridium tetanomorphum has been found to phosphorylate valerate, butyrate, isobutyrate, and propionate. The divalent cation requirement is satisfied with magnesium. The pH optimum lies between 7.4 and 8.3. Growth of the organism was followed using glutamate or histidine as substrate, butyrokinase being formed in each instance. The average dry weight of cells formed per mmole of substrate utilized was 6.8 mg for glutamate and 11.1 mg for histidine. Since both phosphotransbutyrylase and butyrokinase are present in the cells, it is proposed that a significant portion of energy derived from glutamate oxidation by this organism is obtained from butyryl phosphate.