Endoglykanaaseja

Endoglykanaaseja, a term often referring to endoglycosidases or endo-beta-N-acetylglucosaminidases, are enzymes that catalyze the hydrolysis of glycosidic bonds within the core structure of glycans, particularly N-linked glycans. These enzymes play a crucial role in the metabolism and processing of glycoproteins. Unlike exoglycosidases, which cleave sugars from the non-reducing end of a glycan chain, endoglycanases act internally on the oligosaccharide structure.

The primary substrates for endoglycanases are the chitobiose unit found in the core of most N-linked glycans. By breaking this internal linkage, endoglycanases can release large glycan fragments or even individual glycans from the protein backbone. This activity is significant in various biological processes, including protein folding, cellular trafficking, and immune responses. Furthermore, endoglycanases are valuable tools in biochemical research for glycan analysis and glycoprotein modification. They are employed in the study of glycan structure, the generation of homogeneous glycan libraries, and the production of deglycosylated proteins for further investigation. The specificity of different endoglycanases allows for targeted cleavage and manipulation of complex carbohydrate structures.