Summary: Glutamine synthetase (GS) (EC was purified from an deletion containing the GS structural gene. The apparent of the cloned Thiobacillus ferrooxidans GS subunit was approximately 60 000. This indicates a particle for the undissociated enzyme of 720 000, assuming the enzyme is the typical dodecamer. Electron microscopy of of purified GS revealed characteristic disc shaped molecules with central holes. The cloned GS was regulated by Mgor Mn, adenylylation, and nitrogen source but was not affected by feedback modifiers. The GS has a γ-glutamyltransferase isoactivity point of pH 7·71.


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