By R.K. Poole (Eds.)
This quantity is a part of a chain which gives bills of development in microbial biology.
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Extra info for Advances in Microbial Physiology
These strains usually synthesize an active glucose dehydrogenase and under certain growth conditions (for example carbon-limited growth on a mixture of glucose and acetate) they oxidize glucose to gluconate, which accumulates in the growth medium. This is consistent with the observation that when glucose was added to a chemostat culture of A . calcoaceticus growing increased (Mueller and Babel, 1986). on acetate, the yield, Yacetate, In addition to the membrane-bound enzyme, A . 2). , 1995a). 3.
1992b). Usually reconstitution of membrane enzymes into proteoliposomes requires incubation of all the components together. However, in the case of the type 111 quinohaemoprotein alcohol dehydrogenase it was possible to reconstitute an active system by addition of the enzyme to preformed proteoliposomes containing the oxidases. 2). There is some evidence that subunit 11 (the tri-haem cytochrome c) may also be able to mediate electron transfer from membrane glucose dehydrogenase (see below) but the physiological significance of this has yet to be determined.
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. 3 nM. A second approach to the study of the metal ion in the soluble glucose dehydrogenase was developed by Olsthoorn and Duine (1996) who expressed the A . 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.