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. 1970 Apr;102(1):1–5. doi: 10.1128/jb.102.1.1-5.1970

Biochemistry of Coxiella burnetti: 6-Phosphogluconic Acid Dehydrogenase

Thomas L McDonald 1, L Mallavia 1
PMCID: PMC284961  PMID: 4392386

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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