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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1) and, although the overall identity level is not particularly high, i t has been possible to use the sequences of the alcohol dehydrogenase and glucose dehydrogenase, together with the coordinates of the methanol dehydrogenase, to produce reliable model structures of the 'superbarrel regions' (Fig. 5; see also Fig. 10) of these two enzymes. A key feature enabling this to be done is the high level of conservation of the tryptophan-docking motifs which form the basic structure of the propeller superbarrel.
Active enzyme could be formed by incubation with PQQ and a divalent cation, the most effective ions being Cd2+ and Ca2+, followed by Sr2+ and Mn2+; no reconstitution occurred with Mg2+ (Table 4). It should be noted that the percentage values in Table 4 were taken from experiments in which a standard assay was used and reconstitution was for a fixed length of time. These results do not necessarily show that the catalytic activity of the enzyme is highest with the metal ion giving the highest rate in this type of experiment.
1995). PQQ AND QUINOPROTEINS 29 Figure 7 The girdle of tryptophan residues involved in docking the p sheets together. The tryptophan residues involved in docking are shown in spacefill mode and the rest of the chain as backbone. The PQQ prosthetic group is in skeletal form and the calcium ion is shown as a small sphere. the electrophilic C-5 of PQQ. , 1996). ) to the outside of the protein and thence to the electron acceptor. , 1995). Electron transfer to the cytochrome must 30 PAT M. , 1995; Anthony, 1996).