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. 1968 Jul;96(1):55–60. doi: 10.1128/jb.96.1.55-60.1968

Purification and Properties of l-Alanine Dehydrogenase from Desulfovibrio desulfuricans

Geno J Germano a,1, Kenneth E Anderson a
PMCID: PMC252252  PMID: 4298732

Abstract

The l-alanine dehydrogenase from cell-free extracts of Desulfovibrio desulfuricans was purified approximately 56-fold. The Michaelis constants for the substrates of the amination reaction and the pH optima for the reactions catalyzed by this enzyme closely agree with those reported for other l-alanine dehydrogenases. Pyruvate was found to inhibit the amination reaction. The enzyme was absolutely specific for l-alanine and nicotinamide adenine dinucleotide. Its sensitivity to para-chloromecuribenzoate suggests that sulfhydryl groups may be necessary for enzymatic activity. These extracts also contained a nicotinamide adenine dinucleotide phosphate-specific glutamic dehydrogenase which was separated from the l-alanine dehydrogenase during purification.

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Selected References

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