neuraminidase

SYN: sialidase.

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neur·amin·i·dase .n(y)u̇r-ə-'min-ə-.dās, -.dāz n a hydrolytic enzyme that occurs on the surface of the pneumococcus, the orthomyxoviruses, and some paramyxoviruses and that cleaves terminal acetylated neuraminic acids from sugar residues (as in glycoproteins and mucoproteins)

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neu·ra·min·i·dase (noor″ə-minґĭ-dās) an enzyme of the hydrolase class that catalyzes the cleavage of glucosidic linkages between a sialic acid residue and a hexose or hexosamine residue at the nonreducing terminal of oligosaccharides in glycoproteins, glycolipids, and proteoglycans. Cytosolic, plasma membrane, and lysosomal forms of the enzyme exist; deficiency of the latter, an autosomal recessive trait, causes sialidosis; enzyme activity is also lacking in galactosialidosis. Viral neuraminidase found on the surface of influenza viruses enables viral release from the host cell. In EC nomenclature, called exo-α-sialidase. Called also sialidase.