- Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
AMB Express (2014-06-21)
Verena Resch, Jianfeng Jin, Bi-Shuang Chen, Ulf Hanefeld
PMID24949265
ABSTRACT
The Michael hydratase - alcohol dehydrogenase (MhyADH) from Alicycliphilus denitrificans was previously identified as a bi-functional enzyme performing a hydration of α,β-unsaturated ketones and subsequent oxidation of the formed alcohols. The investigations of the bi-functionality were based on a spectrophotometric assay and an activity staining in a native gel of the dehydrogenase. New insights in the recently discovered organocatalytic Michael addition of water led to the conclusion that the previously performed experiments to identify MhyADH as a bi-functional enzyme and their results need to be reconsidered and the reliability of the methodology used needs to be critically evaluated.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Potassium nitrate, BioReagent, suitable for cell culture, suitable for plant cell culture
Sigma-Aldrich
Potassium phosphate dibasic, anhydrous, for luminescence, for molecular biology, BioUltra, ≥99.0% (T)
Sigma-Aldrich
Tetrazolium Blue Chloride, indicator for germination, suitable for microbiology, ≥90% (T)
Sigma-Aldrich
Potassium phosphate monobasic, BioUltra, for molecular biology, anhydrous, ≥99.5% (T)
Sigma-Aldrich
Methylene Blue solution, for microscopy, concentrate according to Ehrlich, concentrated, aqueous solution