Details
| Originalsprache | Englisch |
|---|---|
| Aufsatznummer | e202101625 |
| Fachzeitschrift | CHEMCATCHEM |
| Jahrgang | 14 |
| Ausgabenummer | 7 |
| Frühes Online-Datum | 18 Jan. 2022 |
| Publikationsstatus | Veröffentlicht - 7 Apr. 2022 |
Abstract
Nicotinamide cofactor-dependent oxidoreductases have become a valuable tool for the synthesis of high value chiral compounds. The feasibility of biocatalytic processes involving these enzymes stands and falls with the efficiency of the regeneration of cofactors. In this study, we describe a novel NADPH regeneration method based on the natural thioredoxin electron delivery system. Thioredoxin 1 (Trx1) and thioredoxin reductase (TR) from Thermus thermophilus were characterized for the dithiol-dependent reduction of NADP +, revealing good catalytic activities and a particularly remarkable thermostability. The TR/Trx1 system was then coupled with two representative NADPH-dependent oxidoreductases, alcohol dehydrogenase and cyclohexanone monooxygenase. Reaction conditions for both systems were optimized for reaction yield and selectivity. The results demonstrate the feasibility of the TR/Trx1-system for its application as NADPH regeneration system.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemie (insg.)
- Anorganische Chemie
- Chemie (insg.)
- Physikalische und Theoretische Chemie
- Chemie (insg.)
- Organische Chemie
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in: CHEMCATCHEM, Jahrgang 14, Nr. 7, e202101625, 07.04.2022.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
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TY - JOUR
T1 - Development of a thioredoxin based cofactor regeneration system for NADPH‐dependent oxidoreductases
AU - Zhang, Ningning
AU - Müller, Beatrice
AU - Ørtoft Kirkeby, Tanja
AU - Kara, Selin
AU - Loderer, Christoph
N1 - Funding Information: S.K. and N.Z. thank to Deutsche Forschungsgemeinschaft (DFG), grant agreement No KA 4399/3‐1. S.K. thanks to Aarhus University Research Foundation (AUFF) for the financial support. Open Access funding enabled and organized by Projekt DEAL.
PY - 2022/4/7
Y1 - 2022/4/7
N2 - Nicotinamide cofactor-dependent oxidoreductases have become a valuable tool for the synthesis of high value chiral compounds. The feasibility of biocatalytic processes involving these enzymes stands and falls with the efficiency of the regeneration of cofactors. In this study, we describe a novel NADPH regeneration method based on the natural thioredoxin electron delivery system. Thioredoxin 1 (Trx1) and thioredoxin reductase (TR) from Thermus thermophilus were characterized for the dithiol-dependent reduction of NADP +, revealing good catalytic activities and a particularly remarkable thermostability. The TR/Trx1 system was then coupled with two representative NADPH-dependent oxidoreductases, alcohol dehydrogenase and cyclohexanone monooxygenase. Reaction conditions for both systems were optimized for reaction yield and selectivity. The results demonstrate the feasibility of the TR/Trx1-system for its application as NADPH regeneration system.
AB - Nicotinamide cofactor-dependent oxidoreductases have become a valuable tool for the synthesis of high value chiral compounds. The feasibility of biocatalytic processes involving these enzymes stands and falls with the efficiency of the regeneration of cofactors. In this study, we describe a novel NADPH regeneration method based on the natural thioredoxin electron delivery system. Thioredoxin 1 (Trx1) and thioredoxin reductase (TR) from Thermus thermophilus were characterized for the dithiol-dependent reduction of NADP +, revealing good catalytic activities and a particularly remarkable thermostability. The TR/Trx1 system was then coupled with two representative NADPH-dependent oxidoreductases, alcohol dehydrogenase and cyclohexanone monooxygenase. Reaction conditions for both systems were optimized for reaction yield and selectivity. The results demonstrate the feasibility of the TR/Trx1-system for its application as NADPH regeneration system.
KW - Biocatalysis
KW - Cofactor regeneration
KW - Enzymatic cascades
KW - NADPH
KW - Reductase (TR)
UR - http://www.scopus.com/inward/record.url?scp=85124503977&partnerID=8YFLogxK
U2 - 10.1002/cctc.202101625
DO - 10.1002/cctc.202101625
M3 - Article
VL - 14
JO - CHEMCATCHEM
JF - CHEMCATCHEM
SN - 1867-3880
IS - 7
M1 - e202101625
ER -