Saper Gadiel, Hess Henry
Department of Biomedical Engineering, Columbia University, New York, NY 10027, USA.
PNAS Nexus. 2025 Apr 25;4(5):pgaf134. doi: 10.1093/pnasnexus/pgaf134. eCollection 2025 May.
The catalytic performance of enzymes is largely perceived to be a property of the enzyme itself, altered by environmental conditions, such as temperature and pH. However, the maximal catalytic rates of enzymes differ up to 100-fold between in vivo and in vitro measurements, suggesting that a complex chemical system has additional effects on catalytic performance. In this work, we show that the initial rate of an enzyme can increase 3-fold due to the presence of a second enzyme, which uses the product of the first enzyme as its substrate. This enhancement may originate in an allosteric effect or result from binding competition for the product molecule by the second enzyme.
酶的催化性能在很大程度上被认为是酶本身的一种特性，会受到温度和pH等环境条件的影响而改变。然而，酶的最大催化速率在体内和体外测量之间相差高达100倍，这表明复杂的化学系统对催化性能有额外的影响。在这项工作中，我们表明由于第二种酶的存在，一种酶的初始速率可以提高3倍，第二种酶将第一种酶的产物用作其底物。这种增强可能源于变构效应，或者是由于第二种酶对产物分子的结合竞争所致。
