In vitro activation of NAD‐dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed. Issue 17 (10th June 2014)

• Record Type: Journal Article
• Authors: Ochsner, Andrea M.; Müller, Jonas E.N.; Mora, Carlos A.; Vorholt, Julia A.
• Is Part Of: FEBS letters. Volume 588:Issue 17(2014)
• Page Start: 2993
• Page End: 2999
• Publication Date: 2014-06-10
• Subjects: Adh -- alcohol dehydrogenase -- Mdh -- methanol dehydrogenase -- Nudix -- nucleoside diphosphate-X -- Methylotrophy -- Alcohol dehydrogenase -- Bacillus methanolicus; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.06.008
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract : In vitro activation of B. methanolicus Mdh by Act is not unique. Act specifically improves the catalytic efficiency of Mdh towards methanol. Novel insights into the active sites of Mdh and two other type III Adhs.