TY  - JOUR
AB  - 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.
DA  - 2020
DO  - 10.3390/catal10111281
KW  - alcohol dehydrogenase
KW  - asymmetric synthesis
KW  - biotransformation
KW  - protein crystallography
KW  - protein structure
KW  - short chain dehydrogenase/reductase
LA  - eng
IS  - 11
PY  - 2020
T2  - Catalysts
TI  - Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-29496138
Y2  - 2024-11-22T09:26:38
ER  -