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

Adjogatse, Eyram; Bennett, Josh; Guo, Jingxu; Erskine, Peter T; Wood, Steve P; Wren, Brendan W; Cooper, Jonathan B; (2021) The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile. Acta crystallographica. Section F, Structural biology communications, 77 (Pt 8). pp. 269-274. DOI: https://doi.org/10.1107/S2053230X21007135

Abstract

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.

Additional Information

Item Type	Article
Faculty and Department	Faculty of Infectious and Tropical Diseases > Department of Infection Biology
Research Centre	?? 209951 ??
PubMed ID	34341193
Elements ID	165392