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The X‐ray structure of l ‐threonine dehydrogenase from the common hospital pathogen Clostridium difficile
Author(s) -
Adjogatse Eyram,
Bennett Josh,
Guo Jingxu,
Erskine Peter T.,
Wood Steve P.,
Wren Brendan W.,
Cooper Jonathan B.
Publication year - 2021
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x21007135
Subject(s) - threonine , clostridium difficile , enzyme , biochemistry , pathogen , nad+ kinase , microbiology and biotechnology , biology , clostridium , dehydrogenase , bacteria , chemistry , serine , genetics , antibiotics
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.