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In vitro activation of NAD‐dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed
Author(s) -
Ochsner Andrea M.,
Müller Jonas E.N.,
Mora Carlos A.,
Vorholt Julia A.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.008
Subject(s) - methylotroph , nad+ kinase , biochemistry , alcohol dehydrogenase , methanol dehydrogenase , enzyme , alcohol oxidoreductase , biology , in vitro , dehydrogenase , activator (genetics) , chemistry , gene
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.