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. 1971 May;106(2):571–577. doi: 10.1128/jb.106.2.571-577.1971

Purification and Properties of α-Ketoglutarate Reductase from Micrococcus aerogenes

R F Lerud 1, H R Whiteley 1
PMCID: PMC285132  PMID: 4396793

Abstract

Micrococcus aerogenes grown in media containing glutamate has high levels of glutamate dehydrogenase and α-ketoglutarate reductase. The latter enzyme catalyzes the reversible reduction of α-ketoglutarate to α-hydroxyglutarate in the presence of reduced nicotinamide adenine dinucleotide (NADH). The enzyme has a high specificity for both substrates in either direction and displays Michaelis-Menten kinetics at moderate substrate concentrations. Km values of 0.12 to 0.17 mm α-ketoglutarate and 0.3 mm NADH for the forward reaction were calculated from data obtained at low substrate concentrations. At high concentrations, this reaction was inhibited by both substrates. The reverse reaction, which proceeded at 0.1 to 0.2 times the rate of the forward reactions, was inhibited by one of the products, α-ketoglutarate. Km values for the substrates of this reaction were 10 mm for α-hydroxyglutarate and 1 mm for nicotinamide adenine dinucleotide. α-Ketoglutarate reductase has a molecular weight of 7.5 × 104 to 8.2 × 104 and is composed of identical polypeptide chains with a molecular weight of 3.6 × 104 to 3.8 × 104.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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