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Self-sufficient biocatalytic cascade for the continuous synthesis of danshensu in flow.
Appl Microbiol Biotechnol
January 2025
Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.
A new strategy has been developed to successfully produce the active component danshensu ex vivo. For this purpose, phenylalanine dehydrogenase from Bacillus sphaericus was combined with the novel hydroxyphenylpyruvate reductase from Mentha x piperita, thereby providing an in situ cofactor regeneration throughout the conversion process. The purified enzymes were co-immobilized and subsequently employed in batch biotransformation, resulting in 60% conversion of 10 mM L-dopa within 24 h, with a catalytic amount of NAD as cofactor.
View Article and Find Full Text PDFAllostery and Evolution: A Molecular Journey Through the Structural and Dynamical Landscape of an Enzyme Super Family.
Mol Biol Evol
January 2025
Univ. Grenoble Alpes, CNRS, CEA, IBS, 38000 Grenoble, France.
Allosteric regulation is a powerful mechanism for controlling the efficiency of enzymes. Deciphering the evolutionary mechanisms by which allosteric properties have been acquired in enzymes is of fundamental importance. We used the malate (MalDH) and lactate deydrogenases (LDHs) superfamily as model to elucidate this phenomenon.
View Article and Find Full Text PDFRemote Hydrogen Bonding between Ligand and Substrate Accelerates C-H Bond Activation and Enables Switchable Site Selectivity.
Angew Chem Int Ed Engl
January 2025
RIKEN: Rikagaku Kenkyujo, Center for Sustainable Resource Science, 2-1 Hirosawa, 351-0198, Wako, JAPAN.
Transition-metal-catalyzed selective and efficient activation of an inert C-H bond in an organic substrate is of importance for the development of streamlined synthetic methodologies. An attractive approach is the design of a metal catalyst capable of recognizing an organic substrate through noncovalent interactions to control reactivity and selectivity. We report here a spirobipyridine ligand that bears a hydroxy group that recognizes pyridine and quinoline substrates through hydrogen bonding, and in combination with an iridium catalyst enables site-selective C-H borylation.
View Article and Find Full Text PDFSustainability of Enzymatic Monomer Synthesis: Evaluation via Comparison of Petrochemical and Enzymatic Alkene Epoxidation by Life Cycle Assessment.
ChemSusChem
January 2025
Zittau/Görlitz University of Applied Sciences: Hochschule Zittau/Gorlitz, Faculty of Natural and Environmental Sciences, Theodor-Körner-Allee 16, 02763, Zittau, GERMANY.
Life cycle assessment (LCA) was used, next to green chemistry concepts, to compare the full environmental impacts of the epoxidation of a bio-based monomer, which can be used for the synthesis of vitrimers. On a laboratory scale, the synthesis of the monomer can either be done via a petrochemical route or via an enzymatic reaction pathway. Both reaction pathways were initially optimized to minimize the impact of suboptimal routes on the sustainability evaluation.
View Article and Find Full Text PDFEnzymatic ester bond formation strategies in fungal macrolide skeletons.
Nat Prod Rep
January 2025
College of Pharmaceutical Sciences, Southwest University, 400715 Chongqing, China.
Covering: up to August 2024Macrolides, the core skeletons of numerous marketed drugs and bioactive natural products, have garnered considerable scientific interest owing to their structural diversity and broad spectrum of pharmaceutical activities. The formation of intramolecular ester bonds is a critical biocatalytic step in constructing macrolide skeletons. Here, we summarised enzymatic ester bond formation strategies in fungal polyketide (PK)-type, nonribosomal peptide (NRP)-type, and PK-NRP hybrid-type macrolides.
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