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.

中文翻译：

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医院常见病原菌艰难梭菌L-苏氨酸脱氢酶的X射线结构

在许多原核生物中，苏氨酸代谢的第一步是由苏氨酸脱氢酶 (TDH) 催化，该酶利用 NAD ⁺将其底物氧化为 2-氨基-3-酮丁酸。人类中缺乏功能性 TDH 基因表明该酶的抑制剂可能对依赖该酶的病原体具有治疗潜力。在这里，来自艰难梭菌的TDH已被克隆并过表达，脱辅基酶形式的 X 射线结构已在 2.6 Å 分辨率下确定。