Department of Cell and Molecular Biology (ICM), Uppsala University, Uppsala Biomedical Center, Box 596, S-751 24 Uppsala, Sweden.
FEBS Lett. 2012 Jun 4;586(11):1622-30. doi: 10.1016/j.febslet.2012.04.012. Epub 2012 Apr 25.
In recent years, it has become increasingly clear that many enzymes are catalytically "promiscuous". This can provide a springboard for protein evolution, allowing enzymes to acquire novel functionality without compromising their native activities. We present here a detailed study of Pseudomonas aeruginosa arylsulfatase (PAS), which catalyzes the hydrolysis of a number of chemically distinct substrates, with proficiencies comparable to that towards its native reaction. We demonstrate that the main driving force for the promiscuity is the ability to exploit the electrostatic preorganization of the active site for the native substrate, providing an example of chemistry-driven protein evolution.
近年来，越来越多的证据表明许多酶具有催化“混杂性”。这为蛋白质进化提供了跳板，使酶在不影响其固有活性的情况下获得新的功能。我们在这里介绍了对铜绿假单胞菌芳基硫酸酯酶（PAS）的详细研究，该酶催化水解许多化学性质不同的底物，其效率与对天然反应的效率相当。我们证明，混杂性的主要驱动力是利用活性位点的静电预组织来催化天然底物，这为化学驱动的蛋白质进化提供了一个范例。
