Yao Jianzhuang, Guo Haobo, Chaiprasongsuk Minta, Zhao Nan, Chen Feng, Yang Xiaohan, Guo Hong
Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee , Knoxville, Tennessee 37996, United States.
UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory , Oak Ridge, Tennessee 37830, United States.
Biochemistry. 2015 Sep 1;54(34):5366-75. doi: 10.1021/acs.biochem.5b00638. Epub 2015 Aug 18.
Although one of an enzyme's hallmarks is the high specificity for their natural substrates, substrate promiscuity has been reported more frequently. It is known that promiscuous enzymes generally show different catalytic efficiencies to different substrates, but our understanding of the origin of such differences is still lacking. Here we report the results of quantum mechanical/molecular mechanical simulations and an experimental study of salicylic acid binding protein 2 (SABP2). SABP2 has promiscuous esterase activity toward a series of substrates but shows a high activity toward its natural substrate, methyl salicylate (MeSA). Our results demonstrate that this enzyme may use substrate-assisted catalysis involving the hydroxyl group from MeSA to enhance the activity and achieve substrate discrimination.
尽管酶的一个标志是对其天然底物具有高度特异性,但底物混杂性的报道却更为频繁。已知混杂性酶通常对不同底物表现出不同的催化效率,但我们对这种差异的起源仍缺乏了解。在此,我们报告了水杨酸结合蛋白2(SABP2)的量子力学/分子力学模拟结果及一项实验研究。SABP2对一系列底物具有混杂性酯酶活性,但对其天然底物水杨酸甲酯(MeSA)表现出高活性。我们的结果表明,这种酶可能利用涉及来自MeSA的羟基的底物辅助催化来提高活性并实现底物区分。