Sialic acid
The sialidase is one of the most important enzymes of the sialic acid catabolism. It can cause the removal of sialic acid residues from the cell surface or serum sialoglycoconjugates. Usually, in higher animals, the glycoconjugates that are prone to be degraded are captured by endocytosis. After the fusion of the late endosome with the lysosome, lysosomal sialidases remove sialic acid residues. The activity of these sialidases is based on the removal of "O"-acetyl groups. Free sialic acid molecules are transported to the cytosol through the membrane of the lysosome. There, they can be recycled and activated again to form another nascent glycoconjugate molecule in the Golgi apparatus. Sialic acids can also be degraded to acylmannosamine and pyruvate with the cytosolic enzyme acylneuraminate lyase.