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Статті в журналах з теми "Chemoenzymatic catalysis"

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Автор: Grafiati
Опубліковано: 5 березня 2024

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1

Pauly, Jan, Harald Gröger, and Anant V. Patel. "Developing Multicompartment Biopolymer Hydrogel Beads for Tandem Chemoenzymatic One-Pot Process." Catalysts 9, no. 6 (June 18, 2019): 547. http://dx.doi.org/10.3390/catal9060547.

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Анотація:
Chemoenzymatic processes have been gaining interest to implement sustainable reaction steps or even create new synthetic routes. In this study, we combined Grubbs’ second-generation catalyst with pig liver esterase and conducted a chemoenzymatic one-pot process in a tandem mode. To address sustainability, we encapsulated the catalysts in biopolymer hydrogel beads and conducted the reaction cascade in an aqueous medium. Unfortunately, conducting the process in tandem led to increased side product formation. We then created core-shell beads with catalysts located in different compartments, which notably enhanced the selectivity towards the desired product compared to homogeneously distributing both catalysts within the matrix. Finally, we designed a specific large-sized bead with a diameter of 13.5 mm to increase the diffusion route of the Grubbs’ catalyst-containing shell. This design forced the ring-closing metathesis to occur first before the substrate could diffuse into the pig liver esterase-containing core, thus enhancing the selectivity to 75%. This study contributes to addressing reaction-related issues by designing specific immobilisates for chemoenzymatic processes.
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2

Xu, Yuanfeng, Meng Wang, Bo Feng, Ziyang Li, Yuanhua Li, Hexing Li, and Hui Li. "Dynamic kinetic resolution of aromatic sec-alcohols by using a heterogeneous palladium racemization catalyst and lipase." Catalysis Science & Technology 7, no. 24 (2017): 5838–42. http://dx.doi.org/10.1039/c7cy01954h.

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3

Mertens, M. A. Stephanie, Daniel F. Sauer, Ulrich Markel, Johannes Schiffels, Jun Okuda, and Ulrich Schwaneberg. "Chemoenzymatic cascade for stilbene production from cinnamic acid catalyzed by ferulic acid decarboxylase and an artificial metathease." Catalysis Science & Technology 9, no. 20 (2019): 5572–76. http://dx.doi.org/10.1039/c9cy01412h.

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4

Kadokawa, Jun-ichi. "Enzymatic preparation of functional polysaccharide hydrogels by phosphorylase catalysis." Pure and Applied Chemistry 90, no. 6 (June 27, 2018): 1045–54. http://dx.doi.org/10.1515/pac-2017-0802.

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Анотація:
Abstract This article reviews enzymatic preparation of functional polysaccharide hydrogels by means of phosphorylase-catalyzed enzymatic polymerization. A first topic of this review deals with the synthesis of amylose-grafted polymeric materials and their formation of hydrogels, composed of abundant natural polymeric main-chains, such as chitosan, cellulose, xantham gum, carboxymethyl cellulose, and poly(γ-glutamic acid). Such synthesis was achieved by combining the phosphorylase-catalyzed enzymatic polymerization forming amylose with the appropriate chemical reaction (chemoenzymatic method). An amylose-grafted chitin nanofiber hyrogel was also prepared by the chemoenzymatic approach. As a second topic, the preparation of glycogen hydrogels by the phosphorylase-catalyzed enzymatic reactions was described. When the phosphorylase-catalyzed enzymatic polymerization from glycogen as a polymeric primer was carried out, followed by standing the reaction mixture at room temperature, a hydrogel was obtained. pH-Responsive amphoteric glycogen hydrogels were also fabricated by means of the successive phosphorylase-catalyzed enzymatic reactions.
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5

Horvat, Melissa, Victoria Weilch, Robert Rädisch, Sebastian Hecko, Astrid Schiefer, Florian Rudroff, Birgit Wilding, et al. "Chemoenzymatic one-pot reaction from carboxylic acid to nitrile via oxime." Catalysis Science & Technology 12, no. 1 (2022): 62–66. http://dx.doi.org/10.1039/d1cy01694f.

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Анотація:
We report a new chemoenzymatic cascade starting with aldehyde synthesis by carboxylic acid reductase (CAR) followed by chemical in situ oxime formation and enzymatic dehydration by aldoxime dehydratase (Oxd).
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6

Reymond, Jean-Louis, and Jérémy Boilevin. "Synthesis of Lipid-Linked Oligosaccharides (LLOs) and Their Phosphonate Analogues as Probes To Study Protein Glycosylation Enzymes." Synthesis 50, no. 14 (June 26, 2018): 2631–54. http://dx.doi.org/10.1055/s-0037-1609735.

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Анотація:
Here we review chemical and chemoenzymatic methods for the synthesis of lipid-linked oligosaccharides (LLOs) and their phosphonate analogues, which serve as substrates and inhibitors to investigate the structure and mechanism of protein N-glycosylation enzymes. We emphasize how to overcome the challenges pertaining to the instability and difficult physicochemical properties of this class of compounds.1 Introduction2 LLO Syntheses2.1 Glycosyl Phosphate Syntheses2.2 Glycosyl Phosphonates2.3 Lipid Elongation2.4 Lipid Phosphates2.5 Coupling Reaction Strategies3 Chemoenzymatic Synthesis of Elongated LLOs4 Biological Properties of Synthetic LLOs5 Conclusion
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7

Kuska, Justyna, Freya Taday, Kathryn Yeow, James Ryan, and Elaine O'Reilly. "An in vitro–in vivo sequential cascade for the synthesis of iminosugars from aldoses." Catalysis Science & Technology 11, no. 13 (2021): 4327–31. http://dx.doi.org/10.1039/d1cy00698c.

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Анотація:
Here, we report a chemoenzymatic approach for the preparation of a small panel of biologically important iminosugars from readily available aldoses, employing a transaminase in combination with Gluconobacter oxydans whole cells.
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8

Gao, Liya, Zihan Wang, Yunting Liu, Pengbo Liu, Shiqi Gao, Jing Gao, and Yanjun Jiang. "Co-immobilization of metal and enzyme into hydrophobic nanopores for highly improved chemoenzymatic asymmetric synthesis." Chemical Communications 56, no. 88 (2020): 13547–50. http://dx.doi.org/10.1039/d0cc06431a.

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9

Wu, Yuqi, Jiawei Shen, Dong Yang, Daozhu Xu, Menghan Huang, and Yucai He. "Production of Furfuryl Alcohol from Corncob Catalyzed By CCZU-KF Cell Via Chemoenzymatic Approach." Academic Journal of Science and Technology 6, no. 1 (June 2, 2023): 132–38. http://dx.doi.org/10.54097/ajst.v6i1.9022.

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Анотація:
In this work, the hybrid route of chemo-catalysis and bio-catalysis were used to chemoenzymatically catalyze corncob to produce furfuryl alcohol via sequential conversion with solid acid catalyst at 180 ℃ for 10 min, and E. coli CCZU-KF whole-cell biocatalyst at 35 ℃ for 72 h in 10 vol% choline chloride system. The yield of furfuryl alcohol was 97.7%. This work successfully demonstrated the green and efficient synthesis of furfuryl alcohol production from biomass via chemoenzymatic approach.
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10

Gadler, P., S. M. Glueck, W. Kroutil, B. M. Nestl, B. Larissegger-Schnell, B. T. Ueberbacher, S. R. Wallner, and K. Faber. "Biocatalytic approaches for the quantitative production of single stereoisomers from racemates." Biochemical Society Transactions 34, no. 2 (March 20, 2006): 296–300. http://dx.doi.org/10.1042/bst0340296.

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Strategies for the chemoenzymatic transformation of a racemate into a single stereoisomeric product in quantitative yield have been developed. A range of industrially relevant α-hydroxycarboxylic acids was deracemized in a stepwise fashion via lipase-catalysed enantioselective O-acylation, followed by mandelate racemase-catalysed racemization of the remaining non-reacted substrate enantiomer. Alternatively, aliphatic α-hydroxycarboxylic acids were enzymatically isomerized using whole resting cells of Lactobacillus spp. Enantioselective hydrolysis of rac-sec-alkyl sulphate esters was accomplished using novel alkyl sulphatases of microbial origin. The stereochemical path of catalysis could be controlled by choice of the biocatalyst. Whereas Rhodococcus ruber DSM 44541 and Sulfolobus acidocaldarius DSM 639 act through inversion of configuration, stereo-complementary retaining sulphatase activity was detected in the marine planctomycete Rhodopirellula baltica DSM 10527.
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11

Tiso, Till, Daniel F. Sauer, Klaus Beckerle, Christian C. Blesken, Jun Okuda, and Lars M. Blank. "A Combined Bio-Chemical Synthesis Route for 1-Octene Sheds Light on Rhamnolipid Structure." Catalysts 10, no. 8 (August 4, 2020): 874. http://dx.doi.org/10.3390/catal10080874.

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Анотація:
Here we report a chemoenzymatic approach to synthesize 1-octene from carbohydrates via ethenolysis of rhamnolipids. Rhamnolipids synthesized by P. putida contain a double bond between carbon five and six, which is experimentally confirmed via olefin cross metathesis. Utilizing these lipids in the ethenolysis catalyzed by a Grubbs−Hoveyda-type catalyst selectively generates 1-octene and with good conversions. This study shows the potential of chemoenzymatic approaches to produce compounds for the chemical industry from renewable resources.
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12

Júnior, Aldo Araújo da Trindade, Yan Ferraz Ximenes Ladeira, Alexandre da Silva França, Rodrigo Octavio Mendonça Alves de Souza, Adolfo Henrique Moraes, Robert Wojcieszak, Ivaldo Itabaiana Jr., and Amanda Silva de Miranda. "Multicatalytic Hybrid Materials for Biocatalytic and Chemoenzymatic Cascades—Strategies for Multicatalyst (Enzyme) Co-Immobilization." Catalysts 11, no. 8 (July 31, 2021): 936. http://dx.doi.org/10.3390/catal11080936.

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Анотація:
During recent decades, the use of enzymes or chemoenzymatic cascades for organic chemistry has gained much importance in fundamental and industrial research. Moreover, several enzymatic and chemoenzymatic reactions have also served in green and sustainable manufacturing processes especially in fine chemicals, pharmaceutical, and flavor/fragrance industries. Unfortunately, only a few processes have been applied at industrial scale because of the low stabilities of enzymes along with the problematic processes of their recovery and reuse. Immobilization and co-immobilization offer an ideal solution to these problems. This review gives an overview of all the pathways for enzyme immobilization and their use in integrated enzymatic and chemoenzymatic processes in cascade or in a one-pot concomitant execution. We place emphasis on the factors that must be considered to understand the process of immobilization. A better understanding of this fundamental process is an essential tool not only in the choice of the best route of immobilization but also in the understanding of their catalytic activity.
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13

Tanaka, Tomonari, Ayane Matsuura, Yuji Aso, and Hitomi Ohara. "One-pot chemoenzymatic synthesis of glycopolymers from unprotected sugars via glycosidase-catalysed glycosylation using triazinyl glycosides." Chemical Communications 56, no. 71 (2020): 10321–24. http://dx.doi.org/10.1039/d0cc02838j.

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14

Rajput, Anshul, Arijit De, Amit Mondal, Kiran Das, Biswanath Maity, and Syed Masood Husain. "A biocatalytic approach towards the preparation of natural deoxyanthraquinones and their impact on cellular viability." New Journal of Chemistry 46, no. 7 (2022): 3087–90. http://dx.doi.org/10.1039/d1nj05513e.

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15

Mosley, Sylvester L., Pumtiwitt C. Rancy, Dwight C. Peterson, Justine Vionnet, Rina Saksena, and Willie F. Vann. "Chemoenzymatic synthesis of conjugatable oligosialic acids." Biocatalysis and Biotransformation 28, no. 1 (November 24, 2009): 41–50. http://dx.doi.org/10.3109/10242420903388694.

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16

Yang, Shangjin, Walter Hayden, Kurt Faber, and Herfried Griengl. "Chemoenzymatic Synthesis of (R)-(-)-Citramalic Acid." Synthesis 1992, no. 04 (1992): 365–66. http://dx.doi.org/10.1055/s-1992-26110.

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17

Rutjes, Floris, Stan Groothuys, Brian Kuijpers, Peter Quaedflieg, Harlof Roelen, Roel Wiertz, Richard Blaauw, and Floris van Delft. "Chemoenzymatic Synthesis of Triazole-Linked Glycopeptides." Synthesis 2006, no. 18 (July 25, 2006): 3146–52. http://dx.doi.org/10.1055/s-2006-942509.

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18

Baisch, Gabi, and Reinhold Öhrlein. "Chemoenzymatic Synthesis of Sialyl Lewisx Glycopeptides." Angewandte Chemie International Edition in English 35, no. 16 (September 6, 1996): 1812–15. http://dx.doi.org/10.1002/anie.199618121.

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19

Priyanka, Pragya, Thomas B. Parsons, Antonia Miller, Frances M. Platt, and Antony J. Fairbanks. "Chemoenzymatic Synthesis of a Phosphorylated Glycoprotein." Angewandte Chemie International Edition 55, no. 16 (March 11, 2016): 5058–61. http://dx.doi.org/10.1002/anie.201600817.

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20

Zhang, Jiabin, Ding Liu, Varma Saikam, Madhusudhan R. Gadi, Christopher Gibbons, Xuan Fu, Heliang Song, et al. "Machine‐Driven Chemoenzymatic Synthesis of Glycopeptide." Angewandte Chemie International Edition 59, no. 45 (August 31, 2020): 19825–29. http://dx.doi.org/10.1002/anie.202001124.

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21

Drauz, Karlheinz, Matthias Kottenhahn, Kyriakos Makryaleas, Herbert Klenk та Michael Bernd. "Chemoenzymatic Syntheses ofω-UreidoD-Amino Acids". Angewandte Chemie International Edition in English 30, № 6 (червень 1991): 712–14. http://dx.doi.org/10.1002/anie.199107121.

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22

Li, Shuwei, and Dexing Zeng. "Chemoenzymatic Enrichment of Phosphotyrosine-Containing Peptides." Angewandte Chemie International Edition 46, no. 25 (June 18, 2007): 4751–53. http://dx.doi.org/10.1002/anie.200700633.

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23

Himiyama, Tomoki, and Yasunori Okamoto. "Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications." Molecules 25, no. 13 (June 30, 2020): 2989. http://dx.doi.org/10.3390/molecules25132989.

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Анотація:
Artificial metalloenzymes (ArMs) comprise a synthetic metal complex in a protein scaffold. ArMs display performances combining those of both homogeneous catalysts and biocatalysts. Specifically, ArMs selectively catalyze non-natural reactions and reactions inspired by nature in water under mild conditions. In the past few years, the construction of ArMs that possess a genetically incorporated unnatural amino acid and the directed evolution of ArMs have become of great interest in the field. Additionally, biochemical applications of ArMs have steadily increased, owing to the fact that compartmentalization within a protein scaffold allows the synthetic metal complex to remain functional in a sea of inactivating biomolecules. In this review, we present updates on: (1) the newly reported ArMs, according to their type of reaction, and (2) the unique biochemical applications of ArMs, including chemoenzymatic cascades and intracellular/in vivo catalysis. We believe that ArMs have great potential as catalysts for organic synthesis and as chemical biology tools for pharmaceutical applications.
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24

Dong, Mengmeng, Jiawen Chen, Jiebing Yang, Wei Jiang, Haobo Han, Quanshun Li, and Yan Yang. "Chemoenzymatic synthesis of a cholesterol-g-poly(amine-co-ester) carrier for p53 gene delivery to inhibit the proliferation and migration of tumor cells." New Journal of Chemistry 42, no. 16 (2018): 13541–48. http://dx.doi.org/10.1039/c8nj02574f.

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25

Chênevert, Robert, and Michel Desjardins. "Chemoenzymatic enantioselective synthesis of baclofen." Canadian Journal of Chemistry 72, no. 11 (November 1, 1994): 2312–17. http://dx.doi.org/10.1139/v94-294.

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Анотація:
We report two different chemoenzymatic enantioselective syntheses of baclofen based on the distinction between enantiotopic ester groups in compounds bearing a prochiral centre. In the first approach, the key step is the highly stereoselective enzymatic hydrolysis of dimethyl 3-(4-chlorophenyl)glutarate by chymotrypsin in an aqueous medium. In the second approach, the key step is the enzyme-catalyzed esterification of 2-(4-chloropheny 1)-1,3-propanediol by acetic anhydride in the presence of a lipase in an organic medium.
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26

Chênevert, Robert, Ghodsi Mohammadi-Ziarani, Dave Caron, and Mohammed Dasser. "Chemoenzymatic enantioselective synthesis of (-)-enterolactone." Canadian Journal of Chemistry 77, no. 2 (February 1, 1999): 223–26. http://dx.doi.org/10.1139/v98-231.

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Анотація:
Enterolactone, a lignan isolated from biological fluids of animals and humans, was synthesized via enzymatic desymmetrization of 2-(3-methoxybenzyl)-1,3-propanediol.Key words: enterolactone, synthesis, lipase, desymmetrization, lignan.
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27

Chen, Shaohang, Jiaan Zhang, Zhigang Zeng, Zongjie Dai, Qinhong Wang, Ron Wever, Frank Hollmann, and Wuyuan Zhang. "Chemoenzymatic intermolecular haloether synthesis." Molecular Catalysis 517 (January 2022): 112061. http://dx.doi.org/10.1016/j.mcat.2021.112061.

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28

Korpak, Margarete, та Jörg Pietruszka. "Chemoenzymatic One-Pot Synthesis of γ-Butyrolactones". Advanced Synthesis & Catalysis 353, № 9 (червень 2011): 1420–24. http://dx.doi.org/10.1002/adsc.201100110.

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29

Sigmund, Amy E., Wonpyo Hong, Rafael Shapiro, and Robert DiCosimo. "Chemoenzymatic Synthesis ofcis-4-Hydroxy-D-proline." Advanced Synthesis & Catalysis 343, no. 6-7 (August 2001): 587–90. http://dx.doi.org/10.1002/1615-4169(200108)343:6/7<587::aid-adsc587>3.0.co;2-v.

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30

Thiem, Joachim, and Torsten Wiemann. "Combined Chemoenzymatic Synthesis ofN-Glycoprotein Building Blocks." Angewandte Chemie International Edition in English 29, no. 1 (January 1990): 80–82. http://dx.doi.org/10.1002/anie.199000801.

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31

Thiem, Joachim, and Bernd Sauerbrei. "Chemoenzymatic Syntheses of Sialyloligosaccharides with Immobilized Sialidase." Angewandte Chemie International Edition in English 30, no. 11 (November 1991): 1503–5. http://dx.doi.org/10.1002/anie.199115031.

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32

Wang, Shuaishuai, Qing Zhang, CongCong Chen, Yuxi Guo, Madhusudhan Reddy Gadi, Jin Yu, Ulrika Westerlind, et al. "Facile Chemoenzymatic Synthesis of O-Mannosyl Glycans." Angewandte Chemie International Edition 57, no. 30 (May 18, 2018): 9268–73. http://dx.doi.org/10.1002/anie.201803536.

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33

Meng, Caicai, Aniruddha Sasmal, Yan Zhang, Tian Gao, Chang-Cheng Liu, Naazneen Khan, Ajit Varki, Fengshan Wang, and Hongzhi Cao. "Chemoenzymatic Assembly of Mammalian O-Mannose Glycans." Angewandte Chemie International Edition 57, no. 29 (June 25, 2018): 9003–7. http://dx.doi.org/10.1002/anie.201804373.

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34

Lu, Weigang, Chengli Zong, Pradeep Chopra, Lauren E. Pepi, Yongmei Xu, I. Jonathan Amster, Jian Liu, and Geert-Jan Boons. "Controlled Chemoenzymatic Synthesis of Heparan Sulfate Oligosaccharides." Angewandte Chemie International Edition 57, no. 19 (March 30, 2018): 5340–44. http://dx.doi.org/10.1002/anie.201800387.

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35

Doyon, Tyler J., Jonathan C. Perkins, Summer A. Baker Dockrey, Evan O. Romero, Kevin C. Skinner, Paul M. Zimmerman, and Alison R. H. Narayan. "Chemoenzymatic o-Quinone Methide Formation." Journal of the American Chemical Society 141, no. 51 (December 16, 2019): 20269–77. http://dx.doi.org/10.1021/jacs.9b10474.

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36

Hollmann, Frank, Andreas Kleeb, Katja Otto, and Andreas Schmid. "Coupled chemoenzymatic transfer hydrogenation catalysis for enantioselective reduction and oxidation reactions." Tetrahedron: Asymmetry 16, no. 21 (October 2005): 3512–19. http://dx.doi.org/10.1016/j.tetasy.2005.09.026.

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37

Cao, Yuan, Giang K. T. Nguyen, James P. Tam, and Chuan-Fa Liu. "Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation." Chemical Communications 51, no. 97 (2015): 17289–92. http://dx.doi.org/10.1039/c5cc07227a.

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38

Hitt, David M., Yamina Belabassi, Joyce Suhy, Clifford E. Berkman, and Charles M. Thompson. "Chemoenzymatic resolution of rac-malathion." Tetrahedron: Asymmetry 25, no. 6-7 (April 2014): 529–33. http://dx.doi.org/10.1016/j.tetasy.2014.02.013.

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39

Li, Huanhuan, Sabry H. H. Younes, Shaohang Chen, Peigao Duan, Chengsen Cui, Ron Wever, Wuyuan Zhang, and Frank Hollmann. "Chemoenzymatic Hunsdiecker-Type Decarboxylative Bromination of Cinnamic Acids." ACS Catalysis 12, no. 8 (April 4, 2022): 4554–59. http://dx.doi.org/10.1021/acscatal.2c00485.

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40

Endoma-Arias, Mary Ann, Mariia Makarova, Helen Dela Paz, and Tomas Hudlicky. "Chemoenzymatic Total Synthesis of (+)-Oxycodone from Phenethyl Acetate." Synthesis 51, no. 01 (November 20, 2018): 225–32. http://dx.doi.org/10.1055/s-0037-1611335.

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Анотація:
The stereoselective total synthesis of unnatural (+)-oxy­codone from phenethyl acetate is described. Absolute stereochemistry was established via microbial dihydroxylation of phenethyl acetate with the recombinant strain JM109 (pDTG601A) to the corresponding cis-cyclohexadienediol­ whose configuration provides for the absolute stereo­chemistry of the ring C of (+)-oxycodone. Intramolecular Heck cyclization was employed to establish the quaternary carbon at C-13, along with the dibenzodihydrofuran functionality. The C-14 hydroxyl was installed via SmI2-mediated radical cyclization. The synthesis of (+)-oxy­codone was completed in a total of 13 steps and an overall yield of 1.5%. Experimental and spectral data are provided for all new compounds.
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41

Unverzagt, Carlo. "Chemoenzymatic Synthesis of a Sialylated Undecasaccharide–Asparagine Conjugate." Angewandte Chemie International Edition in English 35, no. 20 (November 1, 1996): 2350–53. http://dx.doi.org/10.1002/anie.199623501.

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42

Johnson, Luke A., Alice Dunbabin, Jennifer C. R. Benton, Robert J. Mart, and Rudolf K. Allemann. "Modular Chemoenzymatic Synthesis of Terpenes and their Analogues." Angewandte Chemie International Edition 59, no. 22 (March 25, 2020): 8486–90. http://dx.doi.org/10.1002/anie.202001744.

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43

Maiti, Sampa, Saikat Manna, Nicholas Banahene, Lucynda Pham, Zhijie Liang, Jun Wang, Yi Xu, et al. "From Glucose to Polymers: A Continuous Chemoenzymatic Process." Angewandte Chemie International Edition 59, no. 43 (August 20, 2020): 18943–47. http://dx.doi.org/10.1002/anie.202006468.

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44

Nikoshvili, Linda Z., and Valentina G. Matveeva. "Recent Progress in Pd-Catalyzed Tandem Processes." Catalysts 13, no. 8 (August 15, 2023): 1213. http://dx.doi.org/10.3390/catal13081213.

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Анотація:
In recent years, Pd-containing catalytic systems for tandem processes have gained special attention due to their enhanced catalytic properties and their possibility of performing several reactions without the necessity of separating the intermediates. In this review, recent progress in Pd-catalyzed tandem processes is considered. Three types of catalytic systems are described: homogeneous catalysts (including immobilized Pd complexes); heterogeneous catalysts supported on oxides, MOFs, COFs, etc., with particular attention to the supports containing acid/base sites; and metal-enzyme catalysts for chemoenzymatic tandem processes applied in fine organic synthesis and biotechnology. For homogeneous Pd-catalyzed reactions, different tandem reactions were considered, i.e., cross-coupling, cyclization, carbonylation, isomerization, alkylation, arylation, etc.
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45

Lima, Gledson Vieira, Marcos Reinaldo da Silva, Thiago de Sousa Fonseca, Leandro Bezerra de Lima, Maria da Conceição Ferreira de Oliveira, Telma Leda Gomes de Lemos, Davila Zampieri, et al. "Chemoenzymatic synthesis of (S)-Pindolol using lipases." Applied Catalysis A: General 546 (September 2017): 7–14. http://dx.doi.org/10.1016/j.apcata.2017.08.003.

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46

Lin, Hening, and Christopher T. Walsh. "A Chemoenzymatic Approach to Glycopeptide Antibiotics." Journal of the American Chemical Society 126, no. 43 (November 2004): 13998–4003. http://dx.doi.org/10.1021/ja045147v.

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47

Angelastro, Antonio, William M. Dawson, Louis Y. P. Luk, E. Joel Loveridge, and Rudolf K. Allemann. "Chemoenzymatic Assembly of Isotopically Labeled Folates." Journal of the American Chemical Society 139, no. 37 (September 6, 2017): 13047–54. http://dx.doi.org/10.1021/jacs.7b06358.

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48

Ko, Kwang-Seuk, Corbin J. Zea, and Nicola L. Pohl. "Strategies for the Chemoenzymatic Synthesis of Deoxysugar Nucleotides: Substrate Binding versus Catalysis." Journal of Organic Chemistry 70, no. 5 (March 2005): 1919–21. http://dx.doi.org/10.1021/jo048424p.

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49

Mathew, Sam, Arunachalam Sagadevan, Dominik Renn, and Magnus Rueping. "One-Pot Chemoenzymatic Conversion of Alkynes to Chiral Amines." ACS Catalysis 11, no. 20 (September 29, 2021): 12565–69. http://dx.doi.org/10.1021/acscatal.1c03474.

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50

Chakraborti, Asit, U. Banerjee, Linga Banoth, Bhukya Chandarrao, and Brahmam Pujala. "Efficient Chemoenzymatic Synthesis of (RS)-, (R)-, and (S)-Bunitrolol." Synthesis 46, no. 04 (December 11, 2013): 479–88. http://dx.doi.org/10.1055/s-0033-1340465.

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