Endo-beta-(1-6)-galactanase

Endo-beta-(1-6)-galactanase is an enzyme that catalyzes the hydrolysis of the (1->6)-beta-D-galactosidic linkages in (1->6)-beta-D-galactan. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is (1->6)-beta-D-galactan 6-galactohydrolase.

Function

Endo-beta-(1-6)-galactanase plays a crucial role in the degradation of complex carbohydrates. It is involved in the breakdown of galactan, a type of polysaccharide that consists of galactose units. This enzyme cleaves the beta-1,6-glycosidic bonds in the galactan molecule, resulting in the release of galactose monomers.

Structure

The structure of endo-beta-(1-6)-galactanase is complex and consists of several protein domains. The active site of the enzyme, where the catalytic activity takes place, is typically located in a cleft or pocket that is lined by amino acid residues that facilitate the binding of the galactan substrate and the catalysis of its hydrolysis.

Biological Significance

Endo-beta-(1-6)-galactanase is significant in various biological processes. It is involved in the metabolism of galactans in plants and some microorganisms. In the human body, it may play a role in the digestion of certain types of dietary fiber.

See Also

• Enzyme
• Hydrolase
• Carbohydrate
• Galactan
• Protein domain