Previous studies on thermal engine models and energy-converting biological systems have shown that some of the parameters affecting their thermodynamic performance also affect their dynamic stability. In some cases, such parameters represent a tradeoff between these two generic properties. In the present work we carry out a similar analysis on a simple model for an enzymatic reaction. Despite its simplicity, this model captures the essential characteristics of numerous biochemical reactions where an endothermic reaction is made possible by coupling it (via an enzyme) with an exothermic reaction. Our results indicate that the global reaction chemical potential gap (􏰁) affects both the thermodynamic properties and stability of the steady state. Larger 􏰁 values imply a higher power output and a higher efficiency, but also a less strongly stable steady state.