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Using the catalytic power of enzymes to
perform highly stereoselective organic transformations has been the
basis of the ever-expanding field of biocatalysis. Enzymes have
evolved over millions of years to be some of the best catalysts
available to chemists. Now, through advances in molecular and
synthetic biology, chemists are able to redesign the active sights of
many enzymes to fit their synthetic needs.
The image by U. Bornscheuer et al. is from an article on the activity of a bacillus subtilis esterase, which appeared in a special issue of ChemCatChem on biocatalysis.
Find all articles on biocatalysis in Wiley Online Library...
Partners in synthesis: This Review provides a guide to the use of biocatalytic methods in the area of chemical synthesis with focus on retrosynthetic considerations and analysis. It is expected to lead to better understanding of the characteristics and distinctions of the two complementary approaches by depicting a road map of challenges and opportunities for the evolution in chemical synthesis.
[Review]
Moritz Hönig, Philipp Sondermann, Nicholas J. Turner, Erick M. Carreira
Angew. Chem. Int. Ed., June 26, 2017, https://doi.org/10.1002/anie.201612462 Read article
[Corrigendum]
Felix Martin Ferroni, Carmien Tolmie, Martha Sophia Smit, Diederik Johannes Opperman
ChemBioChem, June 22, 2017, https://doi.org/10.1002/cbic.201700307 Read article
Enzy-mazing! Synthesis of a selective and competitive HMG-CoA reductase inhibitor rosuvastatin and naturally occurring styryllactone cryptomoscatone E1 has been achieved via Novozyme-435-catalyzed kinetic resolution of racemic syn-ethyl (E)-2-(2,2-dimethyl-6-styryl-1,3-dioxan-4-yl)acetate.
[Communication]
Perla Ramesh, Ramisetti Anjibabu, Yarram Narasimha Reddy, Maddipatla Yedukondalu, Thatikonda Narendar Reddy, Bhaskar Kummari, Atla Raju, Navuluri Srinivasu
Asian J. Org. Chem., June 20, 2017, https://doi.org/10.1002/ajoc.201700228 Read article
Quicker and cleaner: Recombinant glycerate-2-kinase from T. maritima showed excellent selectivity towards phosphorylation of the d-enantiomer of glyceric acid, with no phosphorylation of the l-enantiomer. This straightforward phosphorylation reaction and subsequent product isolation enables the central glycolytic metabolite d-glycerate 2-phosphate to be prepared in fewer reaction steps and with higher purity than chemical routes.
[Full Paper]
Norman Hardt, Birhanu M. Kinfu, Jennifer Chow, Bernhard Schoenenberger, Wolfgang R. Streit, Markus Obkircher, Roland Wohlgemuth
ChemBioChem, June 19, 2017, https://doi.org/10.1002/cbic.201700201 Read article
At pH 5.2 (far below the normal pH optimum of the enzyme), sucrose phosphorylase catalyzes the formation of 2-O-α-d-glucoside of l-ascorbic acid from sucrose and l-ascorbic acid in a single-step, highly efficient, and selective transglucosylation. A “reverse protonation” mechanism that involves a protonated Glu232 underlies the transglucosylation.
[Communication]
Rama Krishna Gudiminchi, Bernd Nidetzky
ChemBioChem, June 05, 2017, https://doi.org/10.1002/cbic.201700215 Read article
Multiple product choices: Cytochrome P450 CYP102A1 (P450 Bm3) variants are used to catalyze the oxidation of ortho-and meta-disubstituted benzenes to a variety of products, with the selective formation of 4-methyl-2-ethylphenol from 3-ethyltoluene, migration of substituents, and the dearomatization product 6-ethyl-6-methylcyclohex-2,4-dienone.
[Full Paper]
Samuel D. Munday, Shaghayegh Dezvarei, Ian C.-K. Lau, Stephen G. Bell
ChemCatChem, June 01, 2017, https://doi.org/10.1002/cctc.201700116 Read article
Two birds with one stone: The reduction of (Z)-β-acylaminonitroalkenes catalyzed by ene-reductases occurs with a high conversion and excellent enantioselectivity to give access to valuable chiral synthons that bear two vicinal nitrogen-containing functional groups.
[Full Paper]
Elisabetta Brenna, Michele Crotti, Francesco G. Gatti, Daniela Monti, Fabio Parmeggiani, Sara Santangelo
ChemCatChem, May 29, 2017, https://doi.org/10.1002/cctc.201700063 Read article
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