<p>The process by which FeaR catalyzes the further oxidation of phenylacetaldehyde into phenylacetic acid (PAA) in the cytoplasm can be broken down into two steps according to the principles of Michaelis-Menten kinetics. The phenylacetic acid produced by the reaction then diffuses out of the cell.</p>
<p>The FeaR-phenylacetaldehyde complex can bind and activate the PTynA promoter. In this case, the concentration of the enzyme-substrate complex <MathJax.Provider>
<span>
<MathJax.Nodeinlineformula={`[FeaR-PA]`}/>
</span>
</MathJax.Provider> is no longer constant, violating the two main assumptions of the Michaelis-Menten equation. However, the relationship between <MathJax.Provider>
<span>
<MathJax.Nodeinlineformula={`K_M`}/>
</span>
</MathJax.Provider> and the rate constants <MathJax.Provider>