Drewke C, Ciriacy M
Institut für Mikrobiologie, Universität Düsseldorf, F.R.G.
Biochim Biophys Acta. 1988 May 6;950(1):54-60. doi: 10.1016/0167-4781(88)90072-3.
We have purified ADHIV, a novel alcohol dehydrogenase (ADH) isozyme in the yeast Saccharomyces cerevisiae, after increasing the normally low amount of ADHIV protein in laboratory strains. This was done by overexpression of the structural gene (ADH4) on a 2micro-based multicopy vector. Characterization of the purified enzyme revealed a dimeric structure as well as a different substrate specificity and pH profile as compared to other alcohol dehydrogenase isozymes. On the other hand, we could demonstrate that ADHIV is activated by zinc ions, like the other yeast alcohol dehydrogenase isozymes, and not by ferrous ions, like a structurally similar alcohol dehydrogenase from the bacterium Zymomonas mobilis.
我们通过增加实验室菌株中通常含量较低的ADHIV蛋白，纯化了酿酒酵母中的一种新型乙醇脱氢酶（ADH）同工酶ADHIV。这是通过在基于2μm的多拷贝载体上过量表达结构基因（ADH4）来实现的。对纯化酶的特性分析表明，与其他乙醇脱氢酶同工酶相比，它具有二聚体结构以及不同的底物特异性和pH谱。另一方面，我们可以证明，ADHIV与其他酵母乙醇脱氢酶同工酶一样，被锌离子激活，而不像来自运动发酵单胞菌的结构相似的乙醇脱氢酶那样被亚铁离子激活。
