1464-98-8Relevant articles and documents
Adenylation Activity of Carboxylic Acid Reductases Enables the Synthesis of Amides
Wood, Alexander J. L.,Weise, Nicholas J.,Frampton, Joseph D.,Dunstan, Mark S.,Hollas, Michael A.,Derrington, Sasha R.,Lloyd, Richard C.,Quaglia, Daniela,Parmeggiani, Fabio,Leys, David,Turner, Nicholas J.,Flitsch, Sabine L.
, p. 14498 - 14501 (2017)
Carboxylic acid reductases (CARs) catalyze the reduction of a broad range of carboxylic acids to aldehydes using the cofactors adenosine triphosphate and nicotinamide adenine dinucleotide phosphate, and have become attractive biocatalysts for organic synthesis. Mechanistic understanding of CARs was used to expand reaction scope, generating biocatalysts for amide bond formation from carboxylic acid and amine. CARs demonstrated amidation activity for various acids and amines. Optimization of reaction conditions, with respect to pH and temperature, allowed for the synthesis of the anticonvulsant ilepcimide with up to 96 % conversion. Mechanistic studies using site-directed mutagenesis suggest that, following initial enzymatic adenylation of substrates, amidation of the carboxylic acid proceeds by direct reaction of the acyl adenylate with amine nucleophiles.
Efficient and general synthesis of 5-(alkoxycarbonyl)methylene-3-oxazolines by palladium-catalyzed oxidative carbonylation of prop-2-ynylamides
Bacchi, Alessia,Costa, Mirco,Gabriele, Bartolo,Pelizzi, Giancarlo,Salerno, Giuseppe
, p. 4450 - 4457 (2002)
A variety of prop-2-ynylamides have been carbonylated under oxidative conditions to give oxazolines, oxazolines with chelating groups, and bisoxazolines bearing an (alkoxycarbonyl)methylene chain at the 5 position in good yields. The cyclization-alkoxycarbonylation process was carried out in alcoholic media at 50-70°C and under 24 bar pressure of 3:1 carbon monoxide/air in the presence of catalytic amounts of 10% Pd/C or PdI2 in conjunction with KI. Cyclization occurred by anti attack of an oxygen function on the palladium-coordinated triple bond, followed by stereospecific alkoxycarbonylation, strictly resulting in E-stereochemistry. The structures of representative oxazolines and bisoxazolines have been determined by X-ray diffraction analysis.
Chemical modifications of poly(vinyl chloride) to poly(vinyl azide) and "clicked" triazole bearing groups for application in metal cation extraction
Ouerghui, Abid,Elamari, Hichem,Dardouri, Mokthar,Ncib, Sana,Meganem, Faouzi,Girard, Christian
, p. 191 - 197 (2016)
Chemical modification of poly(vinyl chloride) (PVC) by the replacement of chlorine atom presents a considerable interest in this work. In the first phase, PVC was partially azided with a sodium azide. Click-chemistry based on Copper (I)-catalyzed Huisgen'
Carboxylic Acid Deoxyfluorination and One-Pot Amide Bond Formation Using Pentafluoropyridine (PFP)
Brittain, William D. G.,Cobb, Steven L.
, p. 5793 - 5798 (2021/08/01)
This work describes the application of pentafluoropyridine (PFP), a cheap commercially available reagent, in the deoxyfluorination of carboxylic acids to acyl fluorides. The acyl fluorides can be formed from a range of acids under mild conditions. We also demonstrate that PFP can be utilized in a one-pot amide bond formation via in situ generation of acyl fluorides. This one-pot deoxyfluorination amide bond-forming reaction gives ready access to amides in yields of ≤94%.
Water Can Accelerate Homogeneous Gold Catalysis
Hashmi, A. Stephen K.,Rudolph, Matthias,Stein, Philipp M.
supporting information, p. 4264 - 4271 (2021/08/03)
A selection of gold-catalyzed reactions was examined in a kinetic study on the influence of water on the rate constant. Two intramolecular reactions and one intermolecular reaction, which proceed via proton transfer and/or protodeauration steps, were inve
Synthesis and structure-activity studies of novel anhydrohexitol-based Leucyl-tRNA synthetase inhibitors
De Ruysscher, Dries,Pang, Luping,Lenders, Stijn M.G.,Cappoen, Davie,Cos, Paul,Rozenski, Jef,Strelkov, Sergei V.,Weeks, Stephen D.,Van Aerschot, Arthur
, (2020/12/02)
Leucyl-tRNA synthetase (LeuRS) is a clinically validated target for the development of antimicrobials. This enzyme catalyzes the formation of charged tRNALeu molecules, an essential substrate for protein translation. In the first step of catalysis LeuRS activates leucine using ATP, forming a leucyl-adenylate intermediate. Bi-substrate inhibitors that mimic this chemically labile phosphoanhydride-linked nucleoside have proven to be potent inhibitors of different members of the aminoacyl-tRNA synthetase family but, to date, they have demonstrated poor antibacterial activity. We synthesized a small series of 1,5-anhydrohexitol-based analogues coupled to a variety of triazoles and performed detailed structure-activity relationship studies with bacterial LeuRS. In an in vitro assay, Kiapp values in the nanomolar range were demonstrated. Inhibitory activity differences between the compounds revealed that the polarity and size of the triazole substituents affect binding. X-ray crystallographic studies of N. gonorrhoeae LeuRS in complex with all the inhibitors highlighted the crucial interactions defining their relative enzyme inhibitory activities. We further examined their in vitro antimicrobial properties by screening against several bacterial and yeast strains. While only weak antibacterial activity against M. tuberculosis was detected, the extensive structural data which were obtained could make these LeuRS inhibitors a suitable starting point towards further antibiotic development.
