Article
Biochemistry & Molecular Biology
Megan Bennett, Laurine Ducrot, Carine Vergne-Vaxelaire, Gideon Grogan
Summary: Native amine dehydrogenases (nat-AmDHs) are a valuable class of enzymes for the sustainable and selective synthesis of chiral amines. MATOUAmDH2, a recently discovered nat-AmDHs, exhibits exceptional catalytic performance and broader substrate scope. The structure of MATOUAmDH2 provides insights for the rational engineering of this and other nat-AmDHs.
Review
Biochemistry & Molecular Biology
Fabio Parmeggiani, Elisabetta Brenna, Danilo Colombo, Francesco G. Gatti, Francesca Tentori, Davide Tessaro
Summary: Ene-reductases from the Old Yellow Enzyme (OYE) superfamily are efficient biocatalytic alternatives for asymmetric reduction of C=C bonds, offering broad substrate tolerance and excellent stereoselectivities. They can produce a wide range of chiral intermediates used in the synthesis of pharmaceuticals, agrochemicals, flavors, fragrances, and fine chemicals.
Article
Chemistry, Multidisciplinary
Ioannis Zachos, Manuel Doering, Georg Tafertshofer, Robert C. Simon, Volker Sieber
Summary: A new stable nicotinamide dinucleotide phosphate cofactor analog, carba-NADP(+), was successfully developed and accepted by a wide range of oxidoreductases. By replacing one ribose oxygen atom in natural NADP(+) with a methylene group, the stability of the cofactor was dramatically enhanced, leading to increased half-life at elevated temperatures. This innovative cofactor opens up possibilities for redox biocatalysis under harsh conditions, as demonstrated by successful testing in over 27 different oxidoreductases.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Review
Chemistry, Multidisciplinary
Victor K. Sharma, Justin M. Hutchison, Alan M. Allgeier
Summary: Enzymatic processes capable of redox reactions are of increasing research interest, with a focus on the regeneration of expensive cofactors required by the enzymes. Alternative methods such as chemical, electrochemical, and photochemical regeneration offer enhanced efficiency and operational simplicity compared to enzymatic regeneration. This comprehensive Review discusses various methods of NAD(P)H cofactor regeneration, quantitatively compares their performance, and identifies barriers and future opportunities for improving the efficiency and sustainability of oxidoreductase processes.
Article
Microbiology
Madeleine Bouzon, Volker Doring, Ivan Dubois, Anne Berger, Gabriele M. M. Stoffel, Liliana Calzadiaz Ramirez, Sophia N. Meyer, Marion Foure, David Roche, Alain Perret, Tobias J. Erb, Arren Bar-Even, Steffen N. Lindner
Summary: This study explores the potential and limits of evolving enzyme cofactor specificity within the cellular context. By using adaptive evolution experiments in an NADPH-auxotrophic strain of E. coli, mutations were found in malic enzyme and dihydrolipoamide dehydrogenase that altered their cofactor preference. However, the study also reveals that biochemical constraints, such as unfavorable thermodynamics, limit the evolution of central metabolism oxidoreductases toward reducing NADP(+).
Article
Chemistry, Multidisciplinary
Xiaoyang Chen, Dannan Zheng, Linye Jiang, Zhiguo Wang, Xinyu Duan, Dong Cui, Shuang Liu, Yuan Zhang, Xiaomin Yu, Jingyan Ge, Jian Xu
Summary: Chiral sulfones are commonly found in pharmaceuticals and bioactive molecules. Existing chemical methods for synthesizing alpha- or beta- chiral sulfones require complicated starting materials and chiral metal complexes. In this study, we developed a photoenzymatic approach using engineered variants of ene reductases as efficient biocatalysts, achieving high yields (up to 92%) and excellent enantioselectivity (up to 99:1) for the synthesis of beta-chiral sulfonyl compounds.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Chemistry, Physical
Eleftheria Diamanti, Javier Santiago-Arcos, Daniel Grajales-Hernandez, Nicolette Czarnievicz, Natalia Comino, Irantzu Llarena, Desire Di Silvio, Aitziber L. Cortajarena, Fernando Lopez-Gallego
Summary: This study conducted multidimensional kinetic analysis on self-sufficient heterogeneous biocatalysts, revealing a thermodynamic equilibrium and the impact of enzyme spatial organization on enzyme performance. Through fluorescence recovery after photobleaching measurements and time-lapse fluorescence microscopy, the study provides insights into the in operando functionality of enzymes within confined spaces.
Article
Chemistry, Multidisciplinary
Chao Shou, Yu-Cong Zheng, Jing-Ru Zhan, Chun-Xiu Li, Jian-He Xu
Summary: A new method has been developed for microbial synthesis of plant-based (-)-menthol, with significantly increased production by replacing inefficient enzymes from Mentha piperita. This lays a reliable foundation for the microbial synthesis of (-)-menthol.
Article
Chemistry, Multidisciplinary
Yu-Fei Ao, Shuxin Pei, Chao Xiang, Marian J. Menke, Lin Shen, Chenghai Sun, Mark Dorr, Stefan Born, Matthias Hohne, Uwe T. Bornscheuer
Summary: We created variants of ATA from Ruegeria sp. (3FCR) with improved catalytic activity and reversed stereoselectivity, and collected a high-quality dataset. We designed a modified one-hot code to describe the effects of substrates and residues within ATAs. Finally, we built a predictor for catalytic activity and stereoselectivity, and applied it for the data-driven design of optimized variants which showed improved activity. We also demonstrated that the model can predict the catalytic activity for ATA variants of another origin by retraining with additional data.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Chemistry, Physical
Danilo Colombo, Elisabetta Brenna, Beatrice Casali, Maria Chiara Ghezzi, Fabio Parmeggiani, Francesca Tentori, Davide Tessaro, Filip Boratynski
Summary: A one-pot chemoenzymatic procedure was developed for the conversion of diol 1 from oleic acid into pelargonic and azelaic acids, with the oxidation of diol 1 into regioisomeric hydroxyketones catalyzed by an alcohol dehydrogenase from Micrococcus luteus. Further oxidative cleavage of the hydroxyketones using NaClO in a biphasic mixture produced pelargonic and azelaic acids in high yield without the need for column chromatography.
Review
Chemistry, Physical
Sahil Verma, Rahul Narayanlal Choudhary, Akash Prakash Kanadje, Uttam Chand Banerjee
Summary: Hydrolases, particularly lipases, play a significant role in the pharmaceutical industry by catalyzing the hydrolysis of ester bonds with high specificity and robustness, making them suitable for various organic synthesis procedures. Genetic engineering has further enhanced the catalytic capabilities of lipases, allowing for the development of customized enzymes for greener biocatalytic drug synthesis. Lipases may also play a key role in developing cascade reactions in organic synthesis, making them a promising candidate for future biocatalytic research in the pharmaceutical industry.
Article
Biochemistry & Molecular Biology
Mozart S. Pereira, Simara S. de Araújo, Ronaldo A. P. Nagem, John P. Richard, Tiago A. S. Brandao
Summary: The activity of salicylate hydroxylase is influenced by different components of its coenzyme FAD, with AMP and ribitol phosphate playing an important role in anchoring the flavin and directing hydroxylation reactions.
BIOORGANIC CHEMISTRY
(2022)
Article
Multidisciplinary Sciences
Ryan A. Herold, Raphael Reinbold, Christopher J. Schofield, Fraser A. Armstrong
Summary: Electrochemical studies reveal that nanoconfinement significantly increases the efficiency of enzyme-catalyzed cascade reactions. By using a nanoporous conducting indium tin oxide film and entrapping Isocitrate dehydrogenase 1 (IDH1), the complete electrochemical oxidation of isocitrate to 2-oxoglutarate is achieved using only the NADP(H) cofactor carried into the electrode pores. The results demonstrate the power of nanoconfinement in facilitating multistep enzyme catalysis and provide insights into the role of nicotinamide cofactors as redox carriers.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Review
Biotechnology & Applied Microbiology
Feng Xue, Changfan Li, Qing Xu
Summary: This review emphasizes the importance of biocatalytic methods in the synthesis of chiral vicinal halohydrins, with a special focus on asymmetric reduction, kinetic resolution, stereoselective biotransformation, asymmetric hydroxylation, asymmetric dehalogenation, and aldehyde condensation.
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Iris S. Teixeira, Andre B. Farias, Bruno A. C. Horta, Humberto M. S. Milagre, Rodrigo O. M. A. de Souza, Uwe T. Bornscheuer, Cintia D. F. Milagre
Summary: This study investigated the influence of an alpha,beta-unsaturated system on the enzymatic reductive amination of ketones catalyzed by amine transaminases. It was found that the wild-type enzymes' reactivity was dramatically reduced by the presence of the double bond, while an engineered variant still maintained high conversion rates and optical purity.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
