Rowell P, Stewart W D
Arch Microbiol. 1975 Sep;107(2):115-24. doi: 10.1007/BF00446830.
The L-alanine dehydrogenase (ADH) of Anabaena cylindrica has been purified 700-fold. It has a molecular weight of approximately 270,000, has 6 sub-units, each of molecular weight approximately 43,000, and shows activity both in the aminating and deaminating directions. The enzyme is NADH/NAD+ specific and oxaloacetate can partially substitute for pyruvate. The Kampp for NAD+ is 14 muM and 60 muM at low and high NAD concentrations respectively.
圆筒鱼腥藻的L-丙氨酸脱氢酶（ADH）已被纯化了700倍。它的分子量约为270,000，有6个亚基，每个亚基的分子量约为43,000，并且在氨基化和脱氨基方向均表现出活性。该酶对NADH/NAD+具有特异性，草酰乙酸可以部分替代丙酮酸。在低NAD浓度和高NAD浓度下，NAD+的米氏常数分别为14μM和60μM。
