Reiner E, Simeon V
Biochim Biophys Acta. 1977 Jan 11;480(1):137-42. doi: 10.1016/0005-2744(77)90328-x.
The kinetics of competition of pairs of two substrates for bovine erythrocyte acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) and horse serum cholinesterase (acylcholine acyl-hydrolase, EC 3.1.1.8) was studied so that the hydrolysis of only one substrate was measured at a time. The substrates were acetylthiocholine, were used as competiting substrates i.e. inhibitors. The substrate inhibition constants (Kss) and Michaelis constants for the reaction of a single substrate were also determined. It was concluded that the substrate inhibition site in the enzyme does not show up in the competition between two substrates.
研究了两种底物对牛红细胞乙酰胆碱酯酶(乙酰胆碱水解酶,EC 3.1.1.7)和马血清胆碱酯酶(酰基胆碱酰基水解酶,EC 3.1.1.8)的竞争动力学,以便每次仅测量一种底物的水解情况。底物为乙酰硫代胆碱,用作竞争底物即抑制剂。还测定了单一底物反应的底物抑制常数(Kss)和米氏常数。得出的结论是,酶中的底物抑制位点在两种底物的竞争中未表现出来。