Bulk chemical 2-methyl-2-butene, one of the main C5 distillates of the petrochemical industry, has scarcely been utilized directly in synthesizing high-value-added fine chemicals. Herein, we use 2-methyl-2-butene as the starting material to develop a palladium-catalyzed highly site- and regio-selective C-3 dehydrogenation reverse prenylation of indoles. This synthetic method features mild reaction conditions, a broad substrate scope, atom- and step-economies.
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http://dx.doi.org/10.1002/chem.202300933 | DOI Listing |
Nat Commun
January 2025
Key Laboratory of Marine Drugs Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, P R China.
Prenylation modifications of natural products play essential roles in chemical diversity and bioactivities, but imidazole modification prenyltransferases are not well investigated. Here, we discover a dimethylallyl tryptophan synthase family prenyltransferase, AuraA, that catalyzes the rare dimethylallylation on the imidazole moiety in the biosynthesis of aurantiamine. Biochemical assays validate that AuraA could accept both cyclo-(L-Val-L-His) and cyclo-(L-Val-DH-His) as substrates, while the prenylation modes are completely different, yielding C2-regular and C5-reverse products, respectively.
View Article and Find Full Text PDFChemistry
January 2025
Department of Chemistry, Indian Institute of Technology Kharagpur Kharagpur 721302, West Bengal, India.
All-carbon quaternary and tertiary stereocenters connected at the C2-position of functionalizable C3-alkylated indole nucleus are commonly occurring frameworks found in many indole alkaloids of medicinal importance. Their direct access is scarcely reported, a long-standing problem, and developing a unique yet simple method can pave the pathway to an entirely different retrosynthetic route for the total synthesis of these alkaloids. Herein, this problem is addressed by developing an unprecedented branch-selective allylation strategy employing a broad range of structurally and electronically different 3-alkenyl-indoles and allylboronic acids.
View Article and Find Full Text PDFMethods Enzymol
November 2024
Centre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, Bangor, United Kingdom; Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Canada. Electronic address:
Microbial carboxylases and decarboxylases play important roles in the global carbon cycle and have many potential applications in biocatalysis and synthetic biology. The widespread family of reversible UbiD-like (de)carboxylases are of particular interest because these enzymes are active against a diverse range of substrates. Several characterized UbiD enzymes have been shown to catalyze reversible (de)carboxylation of aromatic and aliphatic substrates using the recently discovered prenylated FMN (prFMN) cofactor, which is produced by the associated family of UbiX FMN prenyltransferases.
View Article and Find Full Text PDFMethods Enzymol
November 2024
Manchester Institute of Biotechnology, University of Manchester, Manchester, United Kingdom. Electronic address:
The microbial UbiX-UbiD system facilitates the reversible (de)carboxylation of alpha, beta-unsaturated carboxylic acids, including aromatic compounds. The direct C-H carboxylation presents an attractive method for functionalisation and carbon capture but is difficult to achieve under mild conditions. Hence, UbiD-mediated Csp2-H activation can serve as a versatile tool for developing new biocatalytic routes to transform aryl or alkene compounds and carbon dioxide into valuable commodity chemicals.
View Article and Find Full Text PDFInt J Mol Sci
September 2024
Institut de Recherche en Biologie Végétale, Université de Montréal, 4101 Rue Sherbrooke est, Montréal, QC H1X 2B2, Canada.
Cys is one of the least abundant amino acids in proteins. However, it is often highly conserved and is usually found in important structural and functional regions of proteins. Its unique chemical properties allow it to undergo several post-translational modifications, many of which are mediated by reactive oxygen, nitrogen, sulfur, or carbonyl species.
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