McDonald T L, Mallavia L
J Bacteriol. 1970 Apr;102(1):1-5. doi: 10.1128/jb.102.1.1-5.1970.
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.
已对纯化的立克次氏体病原体——伯氏考克斯氏体的制剂进行检测，以确定其使6-磷酸葡萄糖酸脱羧的能力。在提取物中检测到了6-磷酸葡萄糖酸脱氢酶[6-磷酸-D-葡萄糖酸：NADP（烟酰胺腺嘌呤二核苷酸磷酸）氧化还原酶（脱羧），EC 1.1.1.44]，但在伯氏考克斯氏体的全细胞制剂中未检测到。提取物和全细胞均显示没有宿主酶活性的污染。对该酶的部分特性分析表明，它依赖于底物，对NADP具有特异性，并且活性需要镁。立克次氏体酶的最适pH值为8.0。
