Ochsner Andrea M, Müller Jonas E N, Mora Carlos A, Vorholt Julia A
Institute of Microbiology, ETH Zurich, Switzerland.
Institute of Microbiology, ETH Zurich, Switzerland.
FEBS Lett. 2014 Aug 25;588(17):2993-9. doi: 10.1016/j.febslet.2014.06.008. Epub 2014 Jun 10.
In the Gram-positive methylotroph Bacillus methanolicus, methanol oxidation is catalyzed by an NAD-dependent methanol dehydrogenase (Mdh) that belongs to the type III alcohol dehydrogenase (Adh) family. It was previously shown that the in vitro activity of B. methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase. Here we show that this feature is not unique, but more widespread among type III Adhs in combination with Act or other Act-like Nudix hydrolases. In addition, we studied the effect of site directed mutations in the predicted active site of Mdh and two other type III Adhs with regard to activity and activation by Act.
在革兰氏阳性甲基营养菌甲醇芽孢杆菌中，甲醇氧化由一种依赖NAD的甲醇脱氢酶（Mdh）催化，该酶属于III型醇脱氢酶（Adh）家族。先前的研究表明，甲醇芽孢杆菌Mdh的体外活性可被内源性激活蛋白Act（一种Nudix水解酶）增强。在此我们表明，这一特性并非甲醇芽孢杆菌Mdh所独有，而是在与Act或其他类似Act的Nudix水解酶结合的III型Adh中更为普遍。此外，我们研究了Mdh以及另外两种III型Adh的预测活性位点中的定点突变对活性及Act激活作用的影响。
