Anaerobic glycolysis by enzyme preparations of Brucella suis.

The applicability to bacteria of the Embden-Meyerhof scheme of carbohydrate dissimilation has been investigated by many workers, but evidence for the occurrence of phosphorylated hexose intermediates in anaerobic glycolysis by bacteria has been incomplete and indirect. Virtanen and Tikka (1) isolated what they believed to be a hexose monophosphate from a system containing phosphate, glucose, and dried Escherichia coli cells. Phosphoglyceric acid has been isolated as an intermediate in the dissimilation of glucose by Aerobacter, Citrobacter, Escherichia, Propionibacterium, Serratia, and other genera (2-8). Utter and Werkman (9) investigated the aldolase and isomerase equilibria with enzyme preparations of E. coZi. Bard and Gunsalus (10) reported that ferrous ions are required for the function of aldolase prepared from Clostridium perjringens. The occurrence of aldolase suggests that the Embden-Meyerhof system functions in these organisms. The role of phosphate in carbohydrate metabolism has been studied with resting cells of Streptococcus jaecalis by O’Kane and Umbreit (11) and with Propionibactwium pentosaceum by Barker and Lipmann (8). Doudoroff et al. (12) obtained evidence for the formation of glucose-lphosphate, glucose-6-phosphate, and fructose-6-phosphate when dried cell preparations of a non-glucose-fermenting E. coli mutant metabolized maltose under anaerobic conditions. Calorimetric techniques were used, however, to identify and estimate the amounts of phosphorylated intermediates formed. Leloir and coworkers (13-16) investigated the activity of glucose-l ,6diphosphate in the reaction between glucose-l-phosphate and glucose-6phosphate when catalyzed by phosphoglucomutase. Glucose diphosphate was considered the coenzyme in this reaction and was formed by partially purified enzyme preparations from E. coli, Aerobacter aerogenes, and Klebsiella pneumoniae acting on glucose-l-phosphate. These workers postulated that glucose diphosphate was formed by transphosphorylation between 2 molecules of glucose-l-phosphate. The coenzyme involved in the conversion of galactose-l-phosphate to