The sugar phosphate phosphohydrolase activity of Neisseria meningitidis could be significantly repressed by a glucose concentration of 5.5 X lop4 M, and a half-maximal repression was seen with 1.5 X low3 M glucose under the experimental conditions used. This restraint was independent of the Pi concentration, did not require Mg++, Mn++ Fe+++, Na+, K+, or NH4+, and exhibited no correlation with t...

Enzymes are versatile catalysts in laboratories and on an industrial scale; improving their immobilization would be beneficial to broadening their applicability and ensuring their (re)use. Lipid-coated nano-magnets produced by magnetotactic bacteria are suitable for a universally applicable single-step method of enzyme immobilization. By genetically functionalizing the membrane surrounding thes...

Chlorella virus RNA triphosphatase (cvRtp1) is the smallest member of a family of metal-dependent phosphohydrolases that includes the RNA triphosphatases of fungi, protozoa, poxviruses, and baculoviruses. The primary structure of cvRtp1 is more similar to that of the yeast RNA triphosphatase Cet1 than it is to the RNA triphosphatases of other DNA viruses. To evaluate the higher order structural...

Among metallo-dependent phosphatases, ADP-ribose/CDP-alcohol diphosphatases form a protein family (ADPRibase-Mn-like) mainly restricted, in eukaryotes, to vertebrates and plants, with preferential expression, at least in rodents, in immune cells. Rat and zebrafish ADPRibase-Mn, the only biochemically studied, are phosphohydrolases of ADP-ribose and, somewhat less efficiently, of CDP-alcohols an...

Highly purified commercial alkaline phosphatase preparations from Escherichia coli have been shown to catalyze the transfer of a phosphoryl group of inorganic pyrophosphate to the hydroxyl group attached to carbon atom 6 of glucose. Phosphotransferase activity also was detected with relatively crude chicken intestinal alkaline phosphatase preparations. The E. coli enzyme was further characteriz...

1. Incubation of Schistosoma mansoni for 5 min in a phosphate-buffered medium, pH 7.4, released tegumental material containing the following phosphohydrolase activities: alkaline phosphatase, 5'-nucleotidase, glycerol-2-phosphatase, glucose 6-phosphatase, phosphodiesterase and ATPase. 2. Maximum activity of these enzymes was measured at pH 9.5; however, the phosphodiesterase and ATPase activiti...