Affiliation:
1. Department of Bacteriology and Public Health, Washington State University, Pullman, Washington 99163
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
p
H optimum of the rickettsial enzyme is 8.0.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
8 articles.
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