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Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD+ pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein from the ethanol-producing thermophile Geobacillus thermoglucosidasius has been determined to 2.514;Å resolution. This is the first structure to be reported for such a domain. In silico modelling has been carried out to generate a homology model of the aldehyde dehydrogenase domain, and this was subsequently docked with the ADH-domain structure to model the structure of the complete ADHE protein. This model suggests, for the first time, a structural mechanism for the formation of the large multimeric assemblies or 'spirosomes' that are observed for this ADHE protein and which have previously been reported for ADHEs from other organisms.
|Number of pages||12|
|Journal||Acta Crystallographica Section D-Biological Crystallography|
|Publication status||Published - Oct 2013|
Extance, J., Crennell, S. J., Eley, K., Cripps, R., Hough, D. W., & Danson, M. J. (2013). Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in Geobacillus thermoglucosidasius Acta Crystallographica Section D-Biological Crystallography, 69(10), 2104-2115. https://doi.org/10.1107/S0907444913020349