An Enzymatic Toolbox for Cascade Reactions: A Showcase for an In Vivo Redox Sequence in Asymmetric Synthesis

ChemCatChem ◽  
2013 ◽  
Vol 5 (12) ◽  
pp. 3524-3528 ◽  
Author(s):  
Nikolin Oberleitner ◽  
Christin Peters ◽  
Jan Muschiol ◽  
Maria Kadow ◽  
Stefan Saß ◽  
...  
Keyword(s):  
Asymmetric Synthesis ◽  
Cascade Reactions

Asymmetric synthesis and in vivo/in vitro characterization of new hybrid anticonvulsants derived from (2,5-dioxopyrrolidin-1-yl)phenylacetamides

2021 ◽  
Vol 109 ◽  
pp. 104751
Author(s):  
Michał Abram ◽  
Anna Rapacz ◽  
Gniewomir Latacz ◽  
Bartłomiej Szulczyk ◽  
Justyna Kalinowska-Tłuścik ◽  
...  
Keyword(s):  
Asymmetric Synthesis ◽  
In Vitro Characterization

scholarly journals B-973, a Novel α7 nAChR Ago-PAM: Racemic and Asymmetric Synthesis, Electrophysiological Studies, and in Vivo Evaluation

2018 ◽  
Vol 9 (11) ◽  
pp. 1144-1148 ◽  
Author(s):  
Sumanta Garai ◽  
Krishnamohan S. Raja ◽  
Roger L. Papke ◽  
Jeffrey R. Deschamps ◽  
M. Imad Damaj ◽  
...  
Keyword(s):  
Asymmetric Synthesis ◽  
In Vivo Evaluation ◽  
Α7 Nachr ◽  
Electrophysiological Studies

A H2O2-free depot for treating bacterial infection: localized cascade reactions to eradicate biofilms in vivo

Nanoscale ◽  
2018 ◽  
Vol 10 (37) ◽  
pp. 17656-17662 ◽  
Author(s):  
Zhengqing Yan ◽  
Wei Bing ◽  
Chao Ding ◽  
Kai Dong ◽  
Jinsong Ren ◽  
...  
Keyword(s):  
Bacterial Infection ◽  
Cascade Reactions ◽  
Main Components

H2O2-free depots (CaO2/H-G@alginate) can produce hROS in situ through localized cascade reactions, damaging the main components of biofilms.

Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones

2017 ◽  
Vol 398 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Christin Peters ◽  
Florian Rudroff ◽  
Marko D. Mihovilovic ◽  
Uwe T. Bornscheuer
Keyword(s):  
Fusion Protein ◽  
Fusion Proteins ◽  
Reaction Rates ◽  
Cascade Reactions ◽  
Product Formation ◽  
Similar Reaction ◽  
Enzyme Cascade ◽  
Enoate Reductase ◽  
Chiral Lactones

Abstract Nature uses the advantages of fusion proteins for multi-step reactions to facilitate the metabolism in cells as the conversion of substrates through intermediates to the final product can take place more rapidly and with less side-product formation. In a similar fashion, also for enzyme cascade reactions, the fusion of biocatalysts involved can be advantageous. In the present study, we investigated fusion of an alcohol dehydrogenase (ADH), an enoate reductase (ERED) and a Baeyer-Villiger monooxygenase (BVMO) to enable the synthesis of (chiral) lactones starting from unsaturated alcohols as substrates. The domain order and various linkers were studied to find optimal conditions with respect to expression levels and enzymatic activities. Best results were achieved for the ERED xenobiotic reductase B (XenB) from Pseudomonas putida and the cyclohexanone monooxygenase (CHMO) from Acinetobacter sp., whereas none of the ADHs studied could be fused successfully. This fusion protein together with separately supplied ADH resulted in similar reaction rates in in vivo biocatalysis reactions. After 1.5 h we could detect 40% more dihydrocarvone lactone in in vivo reactions with the fusion protein and ADH then with the single enzymes.

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