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The separate roles of PQQ and apo-enzyme syntheses in the regulation of glucose dehydrogenase activity inKlebsiella pneumoniaeNCTC 418

✍ Scribed by R. W. J. Hommes; P. T. D. Herman; P. W. Postma; D. W. Tempest; O. M. Neijssel


Publisher
Springer
Year
1989
Tongue
English
Weight
501 KB
Volume
151
Category
Article
ISSN
0302-8933

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✦ Synopsis


No holoenzyme pyrroloquinoline quinone (PQQ)dependent glucose dehydrogenase and only very low apoenzyme levels could be detected in cells of Klebsiella pneumoniae, growing anaerobically, or carrying out a fumarate or nitrate respiration. Low glucose dehydrogenase activity in some aerobic glucose-excess cultures of K. pneumoniae (ammonia or sulphate limitation) was increased significantly by addition of PQQ, whereas in cells already possessing a high glucose dehydrogenase activity (phosphate or potassium limitation) extra PQQ had almost no effect. These observations indicate that the glucose dehydrogenase activity in K. pneumoniae is modulated by both PQQ synthesis and synthesis of the glucose dehydrogenase apo-enzyme.


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✍ Ed T. Buurman; José L. Boiardi; M. Joost Teixeira de Mattos; Oense M. Neijssel 📂 Article 📅 1990 🏛 Springer 🌐 English ⚖ 435 KB

Magnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 microM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the gl