The X-ray structure of l-threonine dehydrogenase from the common hospital pathogen Clostridium difficile

In many prokaryotes, the first step of threonine metabolism is catalysed by the enzyme threonine dehydrogenase (TDH), which uses NAD+ to oxidize its substrate to 2-amino-3-ketobutyrate. The absence of a functional TDH gene in humans suggests that inhibitors of this enzyme may have therapeutic potential against pathogens which are reliant on this enzyme. Here, TDH from Clostridium difficile has been cloned and overexpressed, and the X-ray structure of the apoenzyme form has been determined at 2.6   Å resolution.

Source: Acta Crystallographica Section F - July 28, 2021 Category: Biochemistry Authors: Adjogatse, E. Bennett, J. Guo, J. Erskine, P.T. Wood, S.P. Wren, B.W. Cooper, J.B. Tags: threonine dehydrogenase Clostridium difficile protein crystallography molecular replacement refinement research communications Source Type: research