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These enzymes are strongly FAD-dependent, and mutations often destabilize FAD-binding motifs or enzyme complexes, impairing fatty acid -oxidation and energy homeostasis

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We determined the crystal structures of Pa DHDPR alone, with its competitive inhibitor (dipicolinate), and the ternary complex of the enzyme with dipicolinate and NADPH, with results showing that only the ternary complex had a fully closed conformation and suggesting that binding of both substrate and nucleotide cofactor is required for enzymatic activity