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| Hauptseite > Publikationsdatenbank > Computer-aided enzymatic retrosynthesis > print |
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| 024 | 7 | _ | |a 10.1038/s41929-021-00582-5 |2 doi |
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| 100 | 1 | _ | |a Rother, Dörte |0 P:(DE-Juel1)144643 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Computer-aided enzymatic retrosynthesis |
| 260 | _ | _ | |a [London] |c 2021 |b Macmillan Publishers Limited, part of Springer Nature |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Biocatalysis makes use of nature’s ability to carry out an incredible number of chemical reactions with excellent selectivity. Since enzymes are biodegradable and operate under mild reaction conditions without producing significant amounts of toxic compounds, biocatalysis can be considered an environmentally friendly alternative to traditional synthesis strategies. The possibility of starting from renewable raw materials is a further advantage when it comes to developing more sustainable production strategies. New enzymes or even entire classes of enzymes are discovered every day. Some of them find their way to industrial scale1,2. In addition, new bioinformatics tools — in combination with molecular biology methods, the integration of non-natural scaffolds and the introduction of complete reaction sequences in microbial hosts — further extend the applicability and diversity of enzymes as catalysts3,4,5. Although, in the past, single-step biocatalysis was mainly investigated in the academic field and applied in industry, the complexity of the reaction pathways and the number of publications with enzymatic multi-step processes are constantly increasing. To get an overview of known biocatalysis pathways/cascades or to get ideas for de novo biotransformations, it has so far been necessary to consult databases or to search in overviews, such as reviews or even textbooks6,7. Recent developments in computer-aided synthesis planning (CASP) facilitate and accelerate synthesis design in synthetic biology as well as organic chemistry. However, enzyme-catalysed steps are under-represented in freely available and commercially chemical CASP tools, and in synthetic biology CASPs the promiscuity of enzymes is not yet fully embedded. This situation has now changed. Writing in Nature Catalysis8, Sabine Flitsch, Nicholas Turner and co-workers disclose an intuitive tool for the computer-aided design of biocatalytic cascades, RetroBioCat, which is freely available at retrobiocat.com. |
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| 700 | 1 | _ | |a Malzacher, Stephan |0 P:(DE-Juel1)178051 |b 1 |u fzj |
| 773 | _ | _ | |a 10.1038/s41929-021-00582-5 |g Vol. 4, no. 2, p. 92 - 93 |0 PERI:(DE-600)2916779-6 |n 2 |p 92 - 93 |t Nature catalysis |v 4 |y 2021 |x 2520-1158 |
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