Enzymatic catalysis is essential to cell survival. In many instances, enzymes that participate in reaction cascades have been shown to assemble into metabolons in response to the presence of the substrate for the first enzyme. However, what triggers metabolon formation has remained an open question. Through a combination of theory and experiments, we show that enzymes in a cascade can assemble via chemotaxis. We apply microfluidic and fluorescent spectroscopy techniques to study the coordinated movement of the first four enzymes of the glycolysis cascade: hexokinase, phosphoglucose isomerase, phosphofructokinase and aldolase. We show that each enzyme independently follows its own specific substrate gradient, which in turn is produced by the preceding enzymatic reaction. Furthermore, we find that the chemotactic assembly of enzymes occurs even under cytosolic crowding conditions.

酶催化对于细胞存活至关重要。在许多情况下，已经显示出参与反应级联的酶响应于第一种酶的底物的存在而组装成代谢产物。然而，引发代谢产物形成的因素仍然是一个悬而未决的问题。通过理论和实验的结合，我们表明级联反应中的酶可以通过趋化性组装。我们应用微流控和荧光光谱技术研究糖酵解级联的前四个酶的协同运动：己糖激酶，磷酸葡萄糖异构酶，磷酸果糖激酶和醛缩酶。我们显示每种酶独立地遵循其自身的特定底物梯度，而后者又是由先前的酶促反应产生的。此外，