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Publication Abstract from PubMed

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 A resolution.

The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile.,Adjogatse E, Bennett J, Guo J, Erskine PT, Wood SP, Wren BW, Cooper JB Acta Crystallogr F Struct Biol Commun. 2021 Aug 1;77(Pt 8):269-274. doi:, 10.1107/S2053230X21007135. Epub 2021 Jul 28. PMID:34341193^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.