cereus houlletii/phosphatase

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Alkaline phosphatase production during sporulation of Bacillus cereus.

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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

Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase.

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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

Effect of metabisulphite on sporulation and alkaline phosphatase in Bacillus subtilis and Bacillus cereus.

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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,

Factors influencing the activity of cellular alkaline phosphatase during growth and sporulation of Bacillus cereus.

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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)

Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle.

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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

Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. I. purification, properties and phosphatase-releasing activity.

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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

ALKALINE PHOSPHATASE REPRESSION BY INORGANIC PHOSPHATE IN BACILLUS ANTHRACIS AND BACILLUS CEREUS.

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Studies on phosphatidylinositol phosphodiesterase (phospholipase C type) of Bacillus cereus. II. In vivo and immunochemical studies of phosphatase-releasing activity.

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Isozyme variability in plants regenerated from calli of Cereus peruvianus (Cactaceae).

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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

Isozyme patterns in callus cultures and in plants regenerated from calli of Cereus peruvianus (Cactaceae).

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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

Interplay of RsbM and RsbK controls the σ(B) activity of Bacillus cereus.

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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.

Partial purification and properties of two phospholipases of Bacillus cereus.

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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

Physiological responses of Bacillus species to concanavalin A. 2. Effect on growth, oxygen uptake, enzyme activities and intracellular cyclic guanosine 3',5'-monophosphate level of B. cereus ATCC 14579.

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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

The kanosamine biosynthetic pathway in Bacillus cereus UW85: Functional and kinetic characterization of KabA, KabB, and KabC.

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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

Physiological studies of a temperature-sensitive sporulation mutant of Bacillus cereus T.

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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

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