High impact information on Propionylthiocholine

• In a practical example we found the light interference to be severe when hydrolysis of propionylthiocholine by plasma cholinesterase (EC 3.1.1.8) was measured after a 20-min incubation [1].
• Wild-type rat BChE catalyzed turnover 2- to 7-fold more rapidly than human BChE, showing the highest turnover with propionylthiocholine (201,000 min(-1)) [2].
• The results showed that the observed cholinesterase activities in the whole embryo may be attributed mainly to acetylcholinesterase with a partial capability to use propionylthiocholine as a second substrate [3].
• In comparison to acetylcholinesterase (AChE) from susceptible adult codling moth, the enzyme of insects resistant to azinphos-methyl has low affinities (higher K(m) values) to the substrates acetylthiocholine (ATCh) and propionylthiocholine [4].
• The maximum velocities (V(max)) for hydrolyzing acetylthiocholine (ATC), propionylthiocholine, and S-butyrylthiocholine were 833.3, 222.2, and 57.5 micromol/min/mg, and the Michaelis constants (K(m)) were 87.9, 26.9, and 195.3 microM, respectively [5].

Anatomical context of Propionylthiocholine

• Final classification of heart muscle cholinesterases was obtained according to both substrate hydrolysis patterns with ASCh, BSCh, acetyl-beta-methylthiocholine and propionylthiocholine, and second-order rate constants for the reaction with organophosphorus inhibitors Mipafox, DFP, and Paraoxon [6].
• Propionylthiocholine is used at the substrate for both plasma butyrylcholinesterase and erythrocyte acetylcholinesterase [7].

Associations of Propionylthiocholine with other chemical compounds

• Wild-type rat BChE had an 8- to 9-fold higher K(m) for the positively charged substrates butyrylthiocholine, acetylthiocholine, propionylthiocholine, benzoylcholine, and cocaine compared with wild-type human BChE [2].
• The cholinesterase activity catalyses the hydrolysis of acetylthiocholine (Km approx. 0.13 mM) and propionylthiocholine (Km approx. 0.26 mM), but not butyrylthiocholine, which is a pure competitive inhibitor (Ki 0.05 mM) [8].
• Kinetics of thiocholine ester hydrolysis showed inhibition by excess substrate which was ascribed to binding of a second substrate molecule, leading to non-productive ternary complex (Km=35 microM, KSS=0.49 mM with propionylthiocholine) [9].
• Whole blood cholinesterase was measured using acetyl-, butyryl- and propionylthiocholine as substrates in 10 healthy adult dogs, cats, horses, pigs, goats, sheep and cows, in order to determine and characterise the cholinesterase activity in whole blood of the main domestic animals [10].

Gene context of Propionylthiocholine

• The procedure is precise and the results obtained from normal and pathological sera show good correlation with those obtained by the alternative procedures employing propionylthiocholine, butyrylthiocholine and benzoylcholine as substrates [11].
• Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(beta-methyl) thiocholine (A beta MTC) and propionylthiocholine (PTC) [12].
• S. mansoni and S. haematobium hydrolyse carboxylic acid esters (10 mM) in decreasing order: phenylacetate (about 2 mumol per hour per mg protein), acetylthiocholine, propionylthiocholine, butyrylthiocholine [13].

References