hydrolase activity, hydrolyzing N-glycosyl compounds

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of any N-glycosyl bond. [GOC:jl]

Hydrolase activity, hydrolyzing N-glycosyl compounds, involves the cleavage of the glycosidic bond between a sugar residue and a non-sugar moiety in an N-glycosylated molecule. This type of hydrolase is crucial for various biological processes, including:

- **Glycoprotein processing:** N-glycans, complex sugar chains attached to proteins, undergo extensive modification and processing in the endoplasmic reticulum and Golgi apparatus. Hydrolases remove specific sugar residues from N-glycans, shaping their structure and influencing their function.

- **Glycolipid degradation:** N-glycosyl compounds can also be attached to lipids, forming glycolipids. Hydrolases break down these glycolipids, releasing free sugars and lipids for cellular metabolism or signaling.

- **Cellular signaling:** Certain N-glycosyl compounds act as signaling molecules, mediating interactions between cells or within the cell. Hydrolases can modulate these signaling pathways by releasing specific sugars from N-glycans, altering their activity.

- **Pathogen defense:** Hydrolases play a role in the immune system's response to pathogens. Some hydrolases can degrade pathogen-derived glycoconjugates, disrupting their ability to infect host cells.

- **Metabolic pathways:** Hydrolases contribute to the breakdown and utilization of complex carbohydrates. They can release sugars from N-glycosyl compounds, making them available for cellular metabolism.

The specificity of hydrolase activity towards N-glycosyl compounds varies depending on the enzyme. Some hydrolases are highly specific for certain sugar residues or glycosidic linkages, while others exhibit broader substrate specificity. This specificity allows for precise regulation of N-glycosylation pathways and ensures proper protein folding, cellular signaling, and other important biological processes.'
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Proteins (1)

Compounds (1)