Germano G J, Anderson K E
J Bacteriol. 1968 Jul;96(1):55-60. doi: 10.1128/jb.96.1.55-60.1968.
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.
从脱硫脱硫弧菌无细胞提取物中获得的L-丙氨酸脱氢酶被纯化了约56倍。该酶催化的胺化反应底物的米氏常数以及反应的最适pH值与其他L-丙氨酸脱氢酶所报道的数值非常吻合。发现丙酮酸会抑制胺化反应。该酶对L-丙氨酸和烟酰胺腺嘌呤二核苷酸具有绝对特异性。它对对氯汞苯甲酸的敏感性表明,巯基可能是酶活性所必需的。这些提取物还含有一种烟酰胺腺嘌呤二核苷酸磷酸特异性谷氨酸脱氢酶,在纯化过程中它与L-丙氨酸脱氢酶分离。