Abstract
The presence of glucose-6-phosphate markedly stimulated the anaerobic utilization of glyoxylate by either cell-free extracts or partially purified enzyme preparations of coli-aerogenes bacteria. The enzymic reduction of glyoxylate to glycollate was found to occur in the presence of TPN with the following substrates; glucose-6-phosphate, glucose plus ATP, gluconate plus ATP, glucose-1-phosphate or malate. The data indicated that the reduction of glyoxylate to glycollate was coupled to the oxidation of glucose-6-phosphate via the hexose monophosphate shunt pathway. It was propounded that the operation of the hexose monophosphate oxidative pathway might be controlled by TPN-linked glyoxylic reductase, and the mechanisms of enzymic regulation in microbial respiration were also discussed.
