113894-26-1Relevant articles and documents
Multiple behaviors in the cleavage of aryl alkanoates by αand β-cyclodextrins. Processes involving two molecules of cyclodextrin
Tee, Oswald S.,Du, Xian-Xian
, p. 620 - 627 (2007/10/02)
The kinetics of ester cleavage of 4-carboxy-2- nitrophenyl alkanoates (1) (C2-C8) and of 2- carboxy-4-nitrophenyl alkanoates (2) (C2, C4,C6, C8) in an aqueous phosphate buffer (pH 11.7) containing α- orβ-cyclodextrin (α- or β-CD) show various types of behavior. Depending on the ester, its acyl chain, and the CD, the kinetics show acceleration (with or without saturation), retardation, acceleration and retardation, retardation and acceleration, or two kinds of acceleration. However, this diversity can be rationalized with simple reaction schemes. Short-chain esters mainly react conventionally through binary CD-ester complexes. For longer chains, some ester/CD combinations exhibit nonproductive 2:1 (CD:ester) binding, whereas other combinations show a cleavage process involving two CD molecules. The latter is most likely due to the attack of a CD (anion) on the 1:1 CD-ester complex or to reaction within a weak 2:1 complex. Modes of transition-state binding are probed using the pseudoequilibrium constants (KTS) introduced in earlier work (Carbohydr. Res. 1989, 192, 181).
A New Class of Phospholipase A2 Substrates: Kinetics of the Phospholipase A2 Catalyzed Hydrolysis of 3-(Acyloxy)-4-nitrobenzoic Acids
Cho, Wonhwa,Markowitz, Michael A.,Kezdy, Ferenc J.
, p. 5166 - 5171 (2007/10/02)
3-(Acyloxy)-4-nitrobenzoic acids were synthesized with acyl groups ranging from butyryl to dodecanoyl.All these compounds yielded monomeric solutions in water with 1.6percent (v/v) acetonitrile in the neutral pH range, and they were hydrolyzed by catalytic amounts of phospholipases A2 from a variety of sources as shown by the spectral change at 425 nm due to the appearance of nitrophenolate ion.Most of the kinetic studies were performed using Agkistrodon piscivorus piscivorus phospholipase A2, but similar results were obtained with porcine pancreatic and Crotalus atrox phospholipase A2.The catalytic reaction requires the presence of Ca2+, but unlike the hydrolysis of lecithins, the hydrolysis of these substrates also occurs in the presence of Ba2+ and Sr2+, while Mg2+ and Zn2+ are not catalytically competent.Increasing the acyl chain length increases the enzymatic rate mainly by enhancing the hydrophobic interaction in the E-Ca2+-S complex.Among structural isomers of the octanoyl compound, 3-nitro-4-(octanoyloxy)benzoic acid shows the highest specificity toward the enzyme, suggesting that it is in this compound that the distance between the negatively charged carboxylate and the reactive ester approximates best that found in the lecithin-enzyme complex.All kinetic characteristics of the enzymatic hydrolysis indicate that the reaction occurs by the same mechanism as that of the hydrolysis of lecithins.The highest catalytic efficiency observed with this series of substrates occurs with 3-dodecanoyl-4-nitrobenzoic acid, and the second-order rate constant of this reaction (kcat/Km = 9.1 x 1E+4 M-1 s-1) is only 1 order of magnitude lower than that of the hydrolysis of egg phosphatidylcholine in unilamellar vesicles.The reactivity of all isomers, especially that of the p-carboxy ester, shows that Ca2+ does not act as a catalyst in the phospholipase A2 catalyzed hydrolysis but rather serves to bind and orient the substrate at the active site of the enzyme.The octanoyl compounds, 1 and 2, are ideally suited for a rapid and sensitive spectrophotometric assay of phospholipases A2, and the conditions for the assay are described.
