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   <subfield code="a">Identification and Characterization of the acoD Gene Encoding a Dihydrolipoamide Dehydrogenase of the Klebsiella pneumoniae Acetoin Dehydrogenase System</subfield>
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   <subfield code="a">The acoD gene, which encodes a dihydrolipoamide dehydrogenase component of the acetoin dehydrogenase enzyme system of Klebsiella pneumoniae was isolated and the nucleotide sequence determined. The gene is capable of encoding a protein of 465 amino acid residues with conserved binding domains for NAD and FAD, and two redox-active cysteine residues. The acoD gene product exhibited a Michaelis constant of 170 μM for NAD, while NADP can not be used as a substrate. The purified enzyme appeared to be a dimer of the acoD gene product. It did not associate tightly with the El and E2 components of either acetoin dehydrogenase or 2-oxoglutarate dehydrogenase to form an active multi-enzyme complex.</subfield>
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