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

By R.K. Poole (Eds.)

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

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There is no suggestion from the model structure or from the primary sequence that there is any hydrophobic region of the protein that could interact with the membrane other than the N-terminal transmembrane segments. 3. The Conserved Sequence that was wrongly identified as the PQQ-binding Domain in Quinoproteins When the primary sequences of these dehydrogenases were first compared it was seen that there was one region of greater identity than any other and it was reasonably concluded that this might represent the one feature known to be common to all PQQ-containing enzymes - their ability to bind PQQ; this region was therefore designated a putative PQQ-binding domain (for review see Anthony, 1992a).

Pneumoniue. In these conditions the yield of dinitrogen fixed per mole of glucose consumed is greater than in strictly anaerobic conditions due to the induction of cytochrome bd which has a very high affinity for oxygen. , 1997). , 1997). This respiration is likely to be by way of glucose dehydrogenase and unlikely to involve the glycolytic enzymes, but some rigorous experiments with appropriate mutants are needed to confirm this. It would also be of interest to determine if synthesis of the glucose dehydrogenase in K .

1989). It catalyses the oxidation of D-glucose, arabinose, galactose, xylose and also the disaccharides lactose, cellobiose and maltose. It is active with Wurster’s blue (pH optimum 9) and 2,6-dichlorophenolindophenol (optimum pH 6 ) , but not with ferricyanide. , 1988). , 1989; Anthony, 1992a), it lacks all their characteristic features including the eight 1 1-residue tryptophan docking motifs which are typical of all the other PQQ-containing quinoprotein dehydrogenases (Anthony, 1996). , 1993).

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