Open AccessBiochemistry ofCoxiella burnetti:6-Phosphogluconic Acid Dehydrogenase
Author(s) -
Thomas L. McDonald,
Louis P. Mallavia
Publication year - 1970
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.102.1.1-5.1970
Subject(s) - biology , biochemistry , enzyme , nicotinamide adenine dinucleotide , dehydrogenase , coxiella burnetii , oxidoreductase , nad+ kinase , nicotinamide adenine dinucleotide phosphate , cofactor , microbiology and biotechnology , enzyme assay , flavin adenine dinucleotide , nicotinamide , oxidase test
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 ofC. 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. Thep H optimum of the rickettsial enzyme is 8.0.
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