Neuraminidase 2 (NEU2)

Neuraminidase 2 (NEU2), also known as sialidase-2, is a cytosolic glycohydrolytic enzyme responsible for cleaving terminal sialic acid residues from glycoproteins and glycolipids, with substrate specificity favoring alpha-(2→3)-linked sialic acids, such as those found on certain gangliosides like GD1a, GT1B, and GM1. The enzyme belongs to the sialidase family (glycoside hydrolases), is structurally characterized by a six-blade β-propeller fold, and demonstrates substrate recognition via a network of active-site residues. NEU2 is involved in critical cell signaling functions, including platelet activation and aggregation through regulated membrane association and desialylation. Diseases linked to NEU2 encompass viral infection (influenza, due to the relevance of neuraminidases), glycoproteinosis, and altered platelet biology, though therapeutic manipulation in humans remains largely experimental.

Other names

Sialidase-2NEU2SIAL2Cytosolic sialidaseN-acetyl-alpha-neuraminidase 2sialidase 2 (cytosolic sialidase)

Competitive inhibition of sialidase catalytic activity, blocking terminal sialic acid removal. Interference with substrate binding and active site function (as demonstrated for DANA inhibitor)