Neuramidase, from A. ureafaciens Inhibitors

Chemical inhibitors of neuraminidase from A. ureafaciens operate through various mechanisms to impede the function of this glycoprotein enzyme. Oseltamivir, for example, mimics the natural substrate of neuraminidase, sialic acid, and binds to the active site of the enzyme. This binding hinders neuraminidase from cleaving sialic acid residues, a key step necessary for the release of viral progeny from host cells. Similarly, Zanamivir and Peramivir interact with the active site, which is crucial for the enzyme's catalytic activity. These inhibitors structurally resemble the transition state of sialic acid during its cleavage, thereby preventing the enzyme from performing its natural function. Laninamivir, another inhibitor, attaches to the active site and brings about a decrease in the enzyme's activity, effectively blocking the liberation of new viral particles.

Continuing with this theme, DANA, a transition state analog inhibitor, binds to neuraminidase's active site, restricting its capacity to cleave sialic acid. The consequence of this inhibition is a reduced ability of the enzyme to aid in the release of viral particles. Oseltamivir carboxylate, the metabolized form of Oseltamivir, targets the enzyme's active site, thereby blocking viral replication. Siastatin B and Fluorosialic acid also play their part as inhibitors by binding to neuraminidase, with the former blocking the cleavage of glycosidic linkages of sialic acid on host cells and the latter acting as a mimic of sialic acid, thereby obstructing the enzyme's role in viral release. Through these diverse but specific interactions, these chemical inhibitors collectively impede the activity of neuraminidase from A. ureafaciens.