exo-alpha-(2->8)-sialidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of alpha-(2->8)-glycosidic linkages of terminal sialic residues in substrates. [EC:3.2.1.18, GOC:mengo_curators]

Exo-alpha-(1-u003e2)-mannanases are glycosyl hydrolases that cleave the alpha-(1-u003e2)-linkages in mannans. Specifically, they hydrolyze the terminal alpha-(1-u003e2)-linked mannose residue from the non-reducing end of mannans. These enzymes play a crucial role in the degradation of mannans, which are complex polysaccharides found in the cell walls of plants, fungi, and bacteria.

Exo-alpha-(1-u003e2)-mannanases are often found in microorganisms, including bacteria and fungi. They are involved in various processes, such as the breakdown of plant cell walls for nutrient acquisition, the production of biofuels from biomass, and the modification of polysaccharides for industrial applications.

The catalytic mechanism of exo-alpha-(1-u003e2)-mannanases involves the formation of a covalent intermediate between the enzyme and the substrate. This intermediate is then hydrolyzed to release the cleaved mannose residue and the enzyme. The active site of exo-alpha-(1-u003e2)-mannanases typically contains an acidic residue, such as glutamate or aspartate, which acts as a general acid catalyst.

These enzymes are important targets for the development of new antibiotics, antifungals, and biocatalysts. Their specific activity against mannans makes them valuable tools for the modification and degradation of these polysaccharides in various industrial applications.
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Proteins (4)

Compounds (30)