neuraminidase /neu·ra·min·i·dase/ (-ah-min´ĭ-dās) an enzyme of the surface coat of myxoviruses that destroys the neuraminic acid of the cell surface during attachment, thereby preventing hemagglutination.
neuraminidase
sialidase [si-al´ĭ-dās]
neu·ra·min·i·dase (n r  -m n -d s, -dz)n. An enzyme that catalyzes the hydrolysis of terminal acylneuraminic residues from oligosaccharides, glycoproteins, and glycolipids. It is present as a surface antigen in myxoviruses. Also called sialidase. |
neuraminidase
[noo͡r′əmē′nədās]
an enzyme that catalyzes the cleavage of N-acetyl neuraminic acid from mucopolysaccharides. A hereditary deficiency of the enzyme causes sialidosis and is associated with galactogialidosis; it is characterized by mental retardation and skeletal changes, especially dysotosis multiplex. Also called sialidase. See also sialidosis.
sialidase [si-al´ĭ-dās]
1. 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. Deficiency of it is an autosomal recessive trait and is seen in sialidosis and galactosialidosis.
2. the enzyme with this activity specifically cleaving sialic acid–containing gangliosides; it is deficient in mucolipidosis IV. Called also neuraminidase.
neuraminidase
1. an enzyme that cleaves the terminal N-acetylneuraminic acid from mucoproteins.
2. a structural component occurring as a spike in the envelope of ortho- and paramyxoviruses.
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