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Publication Abstract from PubMed

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-A crystal structure, this enzyme is a novel member of the beta-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 degrees. 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.

Structural and kinetic properties of a beta-hydroxyacid dehydrogenase involved in nicotinate fermentation.,Reitz S, Alhapel A, Essen LO, Pierik AJ J Mol Biol. 2008 Oct 10;382(3):802-11. Epub 2008 Jul 25. PMID:18680749^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.