R.K. Poole (Eds.)'s Advances in Microbial Physiology PDF

By R.K. Poole (Eds.)

ISBN-10: 0120277409

ISBN-13: 9780120277407

This quantity is a part of a sequence which gives bills of growth in microbial biology.

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Active enzyme may, therefore, form when E. , 1991; Nickerson and Aspedon, 1992). PQQ-dependent oxidation of glucose to gluconate by membrane vesicles of E. , 1985). , 1992). Metabolism by way of glucose dehydrogenase and the Entner-Doudoroff pathway is sufficient to support growth of E. , 1992). Wild-type E. , 1991). The biomass produced was similar to that of cultures grown in the absence of PQQ and the Yglucose decreased because of increased utilization of glucose. In contrast, when the bacteria were grown in the presence of PQQ under glucose limitation there was no accumulation of gluconate; this is because the affinity of glucose for the phosphotransferase system is much greater than that for glucose dehydrogenase.

THE PHYSIOLOGICAL FUNCTIONS OF THE QUINOPROTEIN DEHYDROGENASES I t might be expected that the physiological function of enzymes that oxidize common growth substrates would not merit much discussion, but for the PQQ-containing quinoprotein dehydrogenases this is not the case. To summarize the following discussion in advance, it can be concluded that during growth on methanol and other alcohols as the sole source of carbon and energy the relevant periplasmic dehydrogenases usually play a key role in energy production, catalysing oxidation of the alcohol to the corresponding aldehyde, which is then either further oxidized or assimilated into cell material.

Calcoaceticus gene in E. coli, which does not produce PQQ. The soluble apoenzyme was isolated in the dimeric form, monomerization occurring during gel filtration in the presence of a chelating agent. From a study of reconstitution using the monomer and dimer, it appears that Ca2+ plays a dual role in this enzyme as it is required for dimerization as well as for incorporation of PQQ in a functional form. The ions that could support reconstitution of the wild-type enzyme were also effective in this system (Table 4).

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Advances in Microbial Physiology by R.K. Poole (Eds.)


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