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

Bakonyi D, Toelzer C, Stricker M, Hummel W, Niefind K, Gröger H (2020)
Catalysts 10(11): 1281.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Bakonyi, Daniel; Toelzer, Christine; Stricker, MichaelUniBi; Hummel, WernerUniBi; Niefind, Karsten; Gröger, HaraldUniBi
Abstract / Bemerkung
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.
Stichworte
alcohol dehydrogenase; asymmetric synthesis; biotransformation; protein crystallography; protein structure; short chain dehydrogenase/reductase
Erscheinungsjahr
2020
Zeitschriftentitel
Catalysts
Band
10
Ausgabe
11
Art.-Nr.
1281
eISSN
2073-4344
Finanzierungs-Informationen
Open-Access-Publikationskosten wurden durch die Universität Bielefeld gefördert.
Page URI
https://pub.uni-bielefeld.de/record/2949613

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Bakonyi D, Toelzer C, Stricker M, Hummel W, Niefind K, Gröger H. Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile. Catalysts. 2020;10(11): 1281.
Bakonyi, D., Toelzer, C., Stricker, M., Hummel, W., Niefind, K., & Gröger, H. (2020). Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile. Catalysts, 10(11), 1281. doi:10.3390/catal10111281
Bakonyi, D., Toelzer, C., Stricker, M., Hummel, W., Niefind, K., and Gröger, H. (2020). Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile. Catalysts 10:1281.
Bakonyi, D., et al., 2020. Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile. Catalysts, 10(11): 1281.
D. Bakonyi, et al., “Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile”, Catalysts, vol. 10, 2020, : 1281.
Bakonyi, D., Toelzer, C., Stricker, M., Hummel, W., Niefind, K., Gröger, H.: Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile. Catalysts. 10, : 1281 (2020).
Bakonyi, Daniel, Toelzer, Christine, Stricker, Michael, Hummel, Werner, Niefind, Karsten, and Gröger, Harald. “Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile”. Catalysts 10.11 (2020): 1281.
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2020-12-21T15:50:27Z
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