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- W2073455140 abstract "2-(Hydroxymethyl)glutarate dehydrogenase, the fourth enzyme of the anaerobic nicotinate fermentation pathway of Eubacterium barkeri, catalyzes the NADH-dependent conversion between (S)-2-formylglutarate and (S)-2-(hydroxymethyl)glutarate. As shown by its 2.3-Å crystal structure, this enzyme is a novel member of the β-hydroxyacid dehydrogenase family and adopts a tetrameric architecture with monomers interacting via their C-terminal catalytic domains. The NAD-binding domains protrude heterogeneously from the central, tetrameric core with domain rotation angles differing up to 12°. Kinetic properties of the enzyme, including NADH inhibition constants, were determined. A strong NADH binding in contrast to weaker NAD+ binding of the protein was inferred from fluorometrically determined binding constants for the dinucleotide cofactor. The data support either an Iso Ordered Bi Bi mechanism or a more common Ordered Bi Bi mechanism as found in other dehydrogenases." @default.
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- W2073455140 date "2008-10-01" @default.
- W2073455140 modified "2023-09-26" @default.
- W2073455140 title "Structural and Kinetic Properties of a β-Hydroxyacid Dehydrogenase Involved in Nicotinate Fermentation" @default.
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- W2073455140 doi "https://doi.org/10.1016/j.jmb.2008.07.050" @default.
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