Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile

Daniel Bakonyi, Christine Toelzer, Michael Stricker, Werner Hummel, Karsten Niefind*, Harald Gröger*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

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Alcohol dehydrogenases catalyse the conversion of a large variety of ketone substrates to the corresponding chiral products. Due to their high regio- and stereospecificity, they are key components in a wide range of industrial applications. A novel alcohol dehydrogenase from Comamonas testosteroni (CtADH) was identified in silico, recombinantly expressed and purified, enzymatically and biochemically investigated as well as structurally characterized. These studies revealed a broad pH profile and an extended substrate spectrum with the highest activity for compounds containing halogens as substituents and a moderate activity for bulky–bulky ketones. Biotransformations with selected ketones—performed with a coupled regeneration system for the co-substrate NADPH—resulted in conversions of more than 99% with all tested substrates and with excellent enantioselectivity for the corresponding S-alcohol products. CtADH/NADPH/substrate complexes modelled on the basis of crystal structures of CtADH and its closest homologue suggested preliminary hints to rationalize the enzyme’s substrate preferences
Original languageEnglish
Article number1281
Number of pages14
Issue number11
Publication statusPublished - 4 Nov 2020


  • alcohol dehydrogenase
  • asymmetric synthesis
  • biotransformation
  • protein crystallography
  • protein structure
  • short chain dehydrogenase/reductase

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