Abstract
Abstract Rhodopseudomonas palustris, Glutamine Synthetase Regulation, Adenylylation Glutamine synthetase from Rhodopseudomonas palustris is regulated via an adenylylation/deadenylylation mechanism. The enzyme purified from ammonia-grown cells, released AMP upon treatment with phosphodiesterase, along with drastic changes in its pH and metal dependency. Kinetic parameters for enzyme-substrate interaction were also dependent on the adenylylation state of the enzyme, as was the influence of several nitrogenous feedback inhibitors on the catalytic activity. The adenylylation state of the enzyme was modified in vivo by the availability of ammonia.
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