par Pierard, André ;Wiame, Jean-Marie
Référence Biochimica et biophysica acta, 37, 3, page (490-502)
Publication Publié, 1960-01
Article révisé par les pairs
Résumé : An enzyme responsible for the reversible oxidative deamination of the l(+)-alanine is present in Bacillus subtilis. This enzyme, called l(+)-alanine-dehydrogenase, functions specifically with DPN. The enzyme has been partially purified. It is relatively thermo- and alkali-stable, and is partially inhibited by sulfhydryl reagents. Its optimum pH is 10. Homologues of alanine are very slightly oxidized by it; in order of decreasing activity they are: α-aminobutyric acid, serine, vinylalanine, valine and norvaline. The energetics of the reaction and the Michaelis constants for the substrates have been determined. The specificity of the enzyme makes it suitable for use in the quantitative determination of l(+)-alanine in amounts of 0.1 to 0.3 μmoles. © 1960.