Glutamine synthetase of pseudomonads: some biochemical and physicochemical properties.

Journal of Bacteriology
J M Meyer, E R Stadtman

Abstract

The glutamine synthetases from several Pseudomonas species were purified to homogeneity, and their properties were compared with those reported for the enzymes from Escherichia coli and other gram-negative bacteria. The glutamine synthetase from Pseudomonas fluorescens was unique because it was nearly precipitated quantitatively as a homogeneous protein during dialysis of partially purified preparations against buffer containing 10 mM imidazole (pH 7.0) and 10 mM MnCl2. The glutamine synthetases from Pseudomonas putida and Pseudomonas aeruginosa were purified by affinity chromatography on Affi-blue gel. Dodecamerous forms of the E. coli and P. fluorescens glutamine synthetases had identical mobilities during polyacrylamide gel electrophoresis. Their dissociated subunits, however, migrated differently and were readily separated by electrophoresis on polyacrylamide gels containing 0.1% sodium dodecyl sulfate. This difference in subunit mobilities is not related to the state of adenylylation. Regulation of the Pseudomonas glutamine synthetase activity is mediated by an adenylylation-deadenylylation cyclic cascade system. A sensitive procedure was developed for measuring the average number of adenylylated subunits per enzyme molecu...Continue Reading

Citations

Mar 1, 2003·Archives of Microbiology·Avinash SonawaneKlaus-Heinrich Röhm
Oct 6, 2006·Applied and Environmental Microbiology·Avinash M SonawaneKlaus-Heinrich Röhm
Mar 23, 2017·Proceedings of the National Academy of Sciences of the United States of America·Thang Van NguyenRaymond J Deshaies
Jun 1, 1984·Journal of Bacteriology·R G Donald, R A Ludwig
May 1, 1986·Archives of Biochemistry and Biophysics·J M Meyer, E R Stadtman

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