Kundriutskova L A, Kruglikova R I
Biokhimiia. 1976 Oct;41(10):1773-7.
Hydrolysis of ethers of saturated and unsaturated alcohols and ethers, e.g. phenol and choline, under the action of horse blood serum cholinesterase, was studied. The reactivity towards enzymatic hydrolysis is decreased due to a greater length of the chain in the alcohol residue of the benzoic acid aminoethers; at nCH2 = 4 the compound is a poor substrate. An increase in nydrophobicity of the acyl residue of the ether molecule also leads to a decrease in the Vmax and Km values. In case of cholinesterase substrates, an increase in the molecule hydrophobicity results in an increase of its non-productive absorption on the active surface of the enzyme, which decreases its hydrolysis. Aminobutynol benzoates are hydrolyzed by cholinesterase more rapidly as compared to the ethers of corresponding aminobutanols and their homologs.
研究了在马血清胆碱酯酶作用下，饱和与不饱和醇及醚（如苯酚和胆碱）的醚的水解情况。由于苯甲酸氨基醚的醇残基中链长增加，其对酶促水解的反应性降低；当nCH₂ = 4时，该化合物是一种不良底物。醚分子酰基残基疏水性的增加也会导致Vmax和Km值降低。对于胆碱酯酶底物，分子疏水性的增加会导致其在酶活性表面的非生产性吸附增加，从而降低其水解。与相应氨基丁醇及其同系物的醚相比，氨基丁炔醇苯甲酸酯被胆碱酯酶水解得更快。
