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Cell-bound alkaline phosphatase of Bacillus cereus was produced during vegetative growth and sporulation in a complex medium. Addition of glucose repressed the sporulation process and the amount of enzyme synthesized increased. The time course of alkaline phosphatase production is very similar in
Prokaryotic phosphopentomutases (PPMs) are di-Mn(2+) enzymes that catalyze the interconversion of α-D-ribose 5-phosphate and α-D-ribose 1-phosphate at an active site located between two independently folded domains. These prokaryotic PPMs belong to the alkaline phosphatase superfamily, but previous
The effect of metabisulphite on spore formation and alkaline phosphatase activity/production in Bacillus subtilis and Bacillus cereus was investigated both in liquid and semi-solid substrates. While supplementary nutrient broth (SNB) and sporulation medium (SM) were used as the liquid growth media,
Alkaline phosphatase (EC 3.1.3.1) is synthesized in media with a low phosphate concentration (0.37 mM of total and 19 microM of inorganic phosphate, respectively) already during the exponential phase of growth of Bacillus cereus. The enzyme is repressed by higher phosphate concentrations (3.7 mM)
Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert α-D-ribose 5-phosphate (ribose 5-phosphate) and α-D-ribose 1-phosphate (ribose 1-phosphate). We investigated the reaction mechanism of Bacillus cereus PPM using a combination of structural and
A phosphatidylinositol phosphodiesterase from the culture broth of Bacillus cereus, was purified to a homogeneous state as indicated by polyacrylamide gel electrophoresis, by ammonium sulfate precipitation and chromatography with DEAE-cellulose and CM-Sephadex. The enzyme (molecular weight: 29000
Morphological and isozyme variation was observed among plants regenerated from callus cultures of Cereus peruvianus. Different morphological types of shoots (68%) were observed in 4-year-old regenerated plants, while no distinct morphological variants were observed in plants grown from germinated
Electrophoretic patterns for isocitrate dehydrogenase (IDH; EC 1.1.1.42), acid phosphatase (ACP; EC 3.1.3.2), peroxidase (PER; EC 1.11.1.7), and esterase (EST; EC 3.1.1.1) isozymes were determined in Cereus peruvianus tissues and used as markers of genetic uniformity of calli and of the plants
The alternative transcription factor σ(B) of Bacillus cereus controls the expression of a number of genes that respond to environmental stress. Four proteins encoded in the sigB gene cluster, including RsbV, RsbW, RsbY (RsbU) and RsbK, are known to be essential in the σ(B)-mediated stress response.
Slein, Milton W. (U.S. Army Chemical Corps Biological Laboratories, Fort Detrick, Frederick, Md.) and Gerald F. Logan, Jr. Partial purification and properties of two phospholipases of Bacillus cereus. J. Bacteriol. 85:369-381. 1963.-Culture filtrates of Bacillus cereus contain a phosphatasemia
The effect of the mitogen concanavalin A (Con A) on growth and several physiological aspects of Bacillus cereus ATCC 14579 was investigated. Con A at concentrations ranging from 50 to 750 micrograms/ml stimulated growth (the growth rate increased from 0.52/h to 0.97/h, and final yield increased by
Kanosamine is an aminosugar antibiotic, and component of complex antibiotics such as kanamycin. The biosynthesis of kanosamine varies among different bacteria; best known is a pathway starting from UDP-glucose, but Bacillus subtilis can produce kanosamine in a three-step pathway from glucose
Growth of temperature-sensitive mutant Bacillus cereus T JS22-C occurred normally at the restrictive temperature (37 degrees C), but sporulation was blocked at stage 0. The production of extracellular and intracellular proteases and of alkaline phosphatase occurred at 37 degrees C, but the