Abstract
Purified preparations of the rickettsial agent, Coxiella burnetii, have been examined for their ability to decarboxylate 6-phosphogluconate. The enzyme 6-phosphogluconic acid dehydrogenase [6-phospho-d-gluconate: NADP (nicotinamide adenine dinucleotide phosphate) oxidoreductase (decarboxylating), EC 1.1.1.44] was detected in extracts, but not in whole-cell preparations of C. burnetii. Both extracts and whole cells were shown to be free from contaminating host enzyme activity. Partial characterization of the enzyme has shown that it is substrate-dependent, specific for NADP, and requires magnesium for activity. The pH optimum of the rickettsial enzyme is 8.0.