| Literature DB >> 34341193 |
Eyram Adjogatse1, Josh Bennett1, Jingxu Guo1, Peter T Erskine1, Steve P Wood1, Brendan W Wren2, Jonathan B Cooper1.
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.Entities:
Keywords: Clostridium difficile; molecular replacement; protein crystallography; refinement; threonine dehydrogenase
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Year: 2021 PMID: 34341193 PMCID: PMC8329716 DOI: 10.1107/S2053230X21007135
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.072