Purification and properties of L-alanine dehydrogenase from Desulfovibrio desulfuricans.
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.
D000409:Alanine; D000594:Amino Acid Oxidoreductases; D002474:Cell-Free System; D002623:Chemistry Techniques, Analytical; D002729:Chloromercuribenzoates / Q000494:pharmacology; D002845:Chromatography; D003901:Desulfovibrio / Q000201:enzymology*; D003956:Dialysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD; D011773:Pyruvates / Q000494:pharmacology
D002729:Chloromercuribenzoates; D011773:Pyruvates; D009243:NAD; D000594:Amino Acid Oxidoreductases; D000409:Alanine