1.
Rheumatology (Oxford)
; 62(6): e185-e187, 2023 06 01.
Artículo
en Inglés
| MEDLINE
| ID: mdl-36534829
2.
Acta Crystallogr F Struct Biol Commun
; 77(Pt 8): 269-274, 2021 Aug 01.
Artículo
en Inglés
| MEDLINE
| ID: mdl-34341193
RESUMEN
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 2.6â Å resolution.