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| 001 | 858538 | ||
| 005 | 20220930130203.0 | ||
| 024 | 7 | _ | |a 10.3389/fbioe.2018.00196 |2 doi |
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| 100 | 1 | _ | |a Oeggl, Reinhard |0 P:(DE-Juel1)168384 |b 0 |
| 245 | _ | _ | |a Citrate as Cost-Efficient NADPH Regenerating Agent |
| 260 | _ | _ | |a Lausanne |c 2018 |b Frontiers Media |
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| 520 | _ | _ | |a The economically efficient utilization of NADPH or NADH-dependent enzymes requires the regeneration of consumed reduction equivalents. This cofactor regeneration is classically done via an additional substrate, and if necessary enzyme. We now demonstrate an easy-to-apply cofactor regeneration approach, which can especially be used in screening applications. Simply by applying citrate to a buffer or directly using citrate/-phosphate buffer NADPH can be regenerated by native enzymes of the TCA cycle, practically present in all aerobic living organisms. Apart from viable-culturable cells, this regeneration approach can also be applied with lyophilized cells and even crude cell extracts. This is exemplarily shown for the synthesis of 1 phenylethanol from acetophenone with several oxidoreductases. The mechanism of NADPH regeneration by TCA cycle enzymes was further investigated by a transient isotopic labeling experiment feeding [1,5-13C]citrate. This revealed that the regeneration mechanism can further be optimized by genetic modification of two competing internal citrate metabolization pathways, the glyoxylate shunt and the glutamate dehydrogenase. |
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| 700 | 1 | _ | |a Neumann, Timo |0 P:(DE-Juel1)169334 |b 1 |
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| 700 | 1 | _ | |a Romano, Diego |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Noack, Stephan |0 P:(DE-Juel1)129050 |b 4 |
| 700 | 1 | _ | |a Rother, Dörte |0 P:(DE-Juel1)144643 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.3389/fbioe.2018.00196 |g Vol. 6, p. 196 |0 PERI:(DE-600)2719493-0 |p 196 |t Frontiers in Bioengineering and Biotechnology |v 6 |y 2018 |x 2296-4185 |
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