Purification and Properties of l-Alanine Dehydrogenase from Desulfovibrio desulfuricans
AUTOR(ES)
Germano, Geno J.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=252252Documentos Relacionados
- PURIFICATION AND PROPERTIES OF l-ALANINE DEHYDROGENASE FROM VEGETATIVE CELLS OF BACILLUS CEREUS
- Purification and properties of L-alanine dehydrogenase of the phototrophic bacterium Rhodobacter capsulatus E1F1.
- Expression of an L-alanine dehydrogenase gene in Zymomonas mobilis and excretion of L-alanine.
- Kinetics of l-Alanine Escape from Xylem Vessels
- d-Alanine Oxidase from Escherichia coli: Localization and Induction by l-Alanine
