Mechanism
Proposed transition state for the sialidase mechanism 7 Chemical structures of 4- substituted Neu5Ac2en derivatives 8The enzymatic mechanism of influenza virus sialidase has been studied by Taylor and coworkers, shown in Figure 1. The enzyme catalysis process has four steps. The first step involves the distortion of the α-sialoside from a 2C5 chair conformation (the lowest-energy form in solution) to a pseudoboat conformation when the sialoside binds to the sialidase. The second step leads to an oxocarbocation intermediate, the sialosyl cation. The third step is the formation of Neu5Ac initially as the α-anomer, and then mutarotation and release as the more thermodynamically-stable β-Neu5Ac.
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