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Protein a of quinolinate synthetase is the site of oxygen poisoning of pyridine nucleotide coenzyme synthesis in Escherichia coli
Authors:Bozena Dracyznska-Lusiak  Olen R Brown  
Abstract:De novo biosynthesis of pyridine nucleotide coenzymes in Escherichia coli is initiated by an enzyme complex (quinolinate synthetase) containing protein B which converts l-aspartate into iminoaspartate protein A, which then generates quinolinate on the pathway to the coenzymes. This complex has been shown to be poisoned by hyperbaric oxygen. 7,8 We performed assays made dependent on both proteins B and A versus only protein A, using cell-free extracts of hyperbaric-oxygen poisoned and aerobically grown cells. The specific activities were produced by a similar amounts of 68% and 60%, respectively, when measured in assays made dependent on enzymes B and A versus only protein A that was derived from oxygen-poisoned extract. Thus, protein A is the oxygen-sensitive component.
Keywords:Oxygen toxicity  Oxidative stress  Enzyme inactivation  Pyridine nucleotide coenzymes  Escherichia coli  Free radicals
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