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By R.K. Poole (Eds.)

This quantity is a part of a chain which supplies bills of development in microbial biology.

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One clear difference between these proteins is that there is more ‘space’ in the glucose dehydrogenase active site, perhaps to accommodate the larger substrate. By analogy with the methanol dehydrogenase structure, Asp466 is likely to be involved in base catalysis, initiation of the reaction being by abstraction of a proton from the anomeric hydroxyl of the pyranose ring. As discussed in Section 4, it is possible that the active site of glucose dehydrogenase may sometimes contain big2+ instead of Ca2+, although many of the groups that are involved in coordination to Ca” in methanol dehydrogenase are conserved in the model glucose dehydrogenase.

The reason for the periplasmic location of the quinoprotein dehydrogenases is unclear, but it presumably relates to their nature and/ or to their function. It might be that active enzymes must be assembled outside the cell because of some aspect of PQQ incorporation, or because proper folding of the protein will not occur in a reducing environment. It is probable that all of the quinoproteins contain Ca2+ or Mg2+, and perhaps their periplasmic location avoids the problem of transporting these ions into 36 PAT M.

3. , 1994). Acetic acid bacteria grow in sugary, alcoholic environments and they are typically found on the surfaces of leaves, fruits and alcoholic beverages. Most of the earlier work has concentrated on their use in vinegar production and as spoilers in beers and wines (Swings, 1991). , 1994). Examples of industrial uses include the production of acetic acid from ethanol, gluconic acid from glucose, and sorbose from sorbitol. In the absence of added energy sources acetic acid bacteria are unable to grow on complex media such as peptone, nutrient broth or yeast extract, but they grow well at low to neutral pH when the medium includes an energy source such as ethanol, glucose or glycerol.

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