The components and properties of a phosphoenolpyruvate: glucose phosphotransferase system are reviewed, along with the evidence implicating this system in sugar transport across bacterial membranes. Some possible physiological implications of sugar transport mediated by the phosphotransferase system are also considered. This paper is concerned with a bacterial phosphotransferase system; its properties, and evidence indicating it to be responsible for sugar transport in bacterial cells will be briefly reviewed, and some speculations will be offered concerning the physiological implications of sugar transport via this system.The discovery of the phosphotransferase system resulted from our longstanding interest in the biosynthesis of carbohydrate containing macromolecules (1). The 9-carbon sugar acid, sialic acid, is a frequent component of these macromolecules, and enzymatic degradation of one of the sialic acids (N-acetylneuraminic acid) was found to give pyruvate and N-acetyl-Dmannosamine (2). Studies on the metabolism of the latter sugar led to the discovery of a specific kinase that catalyzes the reaction shown in Fig. 1 ; this kinase is widely distributed in animal tissues (3). Since certain bacterial cells synthesize polymers of N-acetylneuraminic acid, or can metabolize N-acetyl-D-mannosamine, extracts of these cells were examined for the kinase. The sugar was not phosphorylated by the reaction shown in Fig. 1, but it was phosphorylated when phosphoenolpyruvate (PEP) was substituted for ATP. The bacterial system, designated PEP:glycose phosphotransferase system, or simply phosphotransferase system, was found to catalyze the reaction shown in Fig. 2 (4, 5).