Carbamyl phosphate synthesis in Bacillus subtilis

In vitro and "in situ" assays have been developed to test the carbamyl phosphate synthetase (CPSase) activity of a series of pyrimidine-requiring mutants of Bacillus subtilis. The enzyme has been shown to be highly unstable, and was successfully extracted only in the presence of 10% glycer...

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Bibliographic Details
Published in:Biochemical genetics 1975-02, Vol.13 (1-2), p.125-143
Main Authors: Potvin, B, Gooder, H
Format: Article
Language:English
Subjects:
Bacillus subtilis - drug effects
Bacillus subtilis - enzymology
Bacillus subtilis - metabolism
Carbamates - biosynthesis
Carbamyl Phosphate - biosynthesis
Centrifugation, Zonal
Chromatography, Gel
DNA, Bacterial - analysis
Enzyme Activation
Glutamine - metabolism
Hydrogen-Ion Concentration
Muramidase - pharmacology
Mutation
Phosphoribosyl Pyrophosphate - pharmacology
Phosphotransferases - metabolism
Pressure
Pyrimidines - metabolism
Sonication
Transformation, Genetic
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Summary:In vitro and "in situ" assays have been developed to test the carbamyl phosphate synthetase (CPSase) activity of a series of pyrimidine-requiring mutants of Bacillus subtilis. The enzyme has been shown to be highly unstable, and was successfully extracted only in the presence of 10% glycerol and 1 mM dithiothreitol (Cleland's reagent). It loses activity rapidly when sonicated or when treated with lysozyme. Genetic studies, using mutants, indicate that B. subtilis may possess two CPSases. This possibility and its physiological consequences were probed enzymatically. CPSase activity has been shown to undergo inhibition by both uridine triphosphate and dihydroorotate; activation has been demonstrated in response to phosphoribosyl pyrophosphate (PRPP) and (to a lesser extent) ornithine.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00486011