Regulation of Glucosylation of Teichoic Acid

Analysis of purified phosphoglucomutase (EC 2.7.5.1) demonstrated that the two distinct chromatographic forms consisted of dimers with an approximate molecular weight of 130,000. Both phosphoglucomutase I and II spontaneously dissociated at pH 6.5 in low concentrations of Mg2+. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the monomers of phosphoglucomutase I and phosphoglucomutase II are indistinguishable. However, these two forms of the enzyme differed in specific activity, rate of inactivation at 50°, and Km. A 50 % inhibition of both forms occurred with 1 to 2 x 10-5 m UTP or GTP. A model for the regulation of phosphoglucomutase in Bacillus subtilis was presented.