Pessione E, Pergola L, Cavaletto M, Giunta C, Trotta A, Vanni A
Dipartimento di Biologia Animale, Università, Torino.
Ital J Biochem. 1990 Mar-Apr;39(2):71-82.
The enzyme ADH1 has been extracted and purified from the budding yeast Kluyveromyces marxianus, and its enzymatic activity has been compared, with the ADH1 extracted and purified in the same way from the well known yeast Saccharomyces cerevisiae. K. marxianus ADH1 has an optimal temperature higher than the S. cerevisiae enzyme (45-50 degrees vs 35 degrees C), a better stability to pH variations in the oxidative reaction (pH optimum 7.5), a lower Michaelis constant for acetaldehyde, and a good catalytic activity both for fermentative and oxidative reactions. In fact, while in Saccharomyces the constants ratio (velocity constant fermentation/velocity constant oxidation) is about 20,000, in Kluyveromyces the same ratio is only 15. Even if these two Genera are quite related (they belong to the same subfamily) it seems that their ADH1s possess different catalytic properties.
已从马克斯克鲁维酵母（Kluyveromyces marxianus）这种出芽酵母中提取并纯化了乙醇脱氢酶1（ADH1），并将其酶活性与以同样方式从著名的酿酒酵母（Saccharomyces cerevisiae）中提取并纯化的ADH1进行了比较。马克斯克鲁维酵母的ADH1具有比酿酒酵母的酶更高的最适温度（45 - 50摄氏度对35摄氏度），在氧化反应中对pH变化具有更好的稳定性（最适pH 7.5），对乙醛的米氏常数更低，并且对发酵和氧化反应均具有良好的催化活性。实际上，在酿酒酵母中常数比（发酵速度常数/氧化速度常数）约为20,000，而在马克斯克鲁维酵母中该比值仅为15。即使这两个属关系密切（它们属于同一亚科），但似乎它们的ADH1具有不同的催化特性。
