Physiological function of periplasmic hexose phosphatase in Salmonella typhimurium.
Hydrolysis of sugar phosphates by crude and purified preparations of periplasmic hexose phosphatase from Salmonella typhimurium followed Michaelis-Menten kinetics. The enzyme bound glucose 1-phosphate with high affinity (Km = 10 microM) but bound glucose 6-phosphate with low affinity (Km = 2,000 microM). The order of substrate affinities was glucose 1-phosphate greater than mannose 1-phosphate = galactose 1-phosphate greater than fructose 1-phosphate greater than glucose 6-phosphate. These results and others suggest that the physiological function of the enzyme is the periplasmic hydrolysis of hexose 1-phosphates.
D003593:Cytoplasm / Q000201:enzymology; D005636:Fructosephosphates / Q000378:metabolism; D005695:Galactosephosphates / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D007700:Kinetics; D008360:Mannosephosphates / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology*; D013379:Substrate Specificity
D005636:Fructosephosphates; D005695:Galactosephosphates; D005958:Glucosephosphates; D008360:Mannosephosphates; C024254:hexose phosphatase; D010744:Phosphoric Monoester Hydrolases