With the rapid development and complex challenges of chemical substances, new drug synthesis pathways are usually the most effective.3301-94-8,6-Butyltetrahydro-2H-pyran-2-one,as a common compound, the synthetic route is as follows.
General procedure: The lactonase, phosphotriesterase, and esterase hydrolyses of GkaP were monitored by absorbance changes in a UV-2550 spectrophotometer (Shimadzu, Kyoto, Japan) at a constant temperature of 75C with 1 mL reaction volumes (path length = 1cm). Analysis of reaction samples for each substrate was performed at a constant enzyme concentration. The delta-decanolactone substrate was dissolved in dimethyl sulfoxide (DMSO), whereas the p-nitrophenylcaprylate and OP substrates in acetonitrile as stock solutions. For enzymatic kinetics assay, aliquots of the stock were added to the reaction buffer for defined concentrations. The hydrolysis of lactone was monitored using a pH-sensitive colorimetric assay [33]. Briefly, the reactions were performed in 2.5 mM Bicine (pH 8.3) containing 0.2MNaCl, 0.2 mM cresol purple, and 0.02-20 mM lactone substrate. Upon mixture of the substrate with the enzyme, the decrease inabsorbance was monitored at 577 nm (epsilon577 = 47300 M-1cm-1, 1%DMSO). The enzyme was diafiltrated with 10 mM bicine (pH 8.3), with a PD-10 column (GE Healthcare, Shanghai, China) before use. Kinetic measurements with p-nitrophenyl caprylate (pNPC8), and ethyl-paraoxon were performed in 50 mM phosphate buffer (pH 8.0). The reaction rates were monitored bythe release of p-nitrophenol (epsilon405 = 16000M-1cm-1, 2% acetonitrile). The initial rates were corrected for the background rate of spontaneous hydrolysis in the absence of enzymes, which were subtracted from the enzymatic rates. The kinetic parameters (kcat, Km) were obtained byfitting the data to the Michaelis-Menten equation [V = S¡ÁE¡Ákcat/(S+Km)] or to the pseudo first-order form of it at S<
Tetrahydropyran – Wikipedia
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