Page last updated: 2024-10-24

beta-N-acetylglucosaminidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-beta-D-glucosaminides. [EC:3.2.1.52, MetaCyc:3.2.1.52-RXN]

Beta-N-acetylglucosaminidase (NAGase) activity refers to the enzymatic hydrolysis of the glycosidic bond between a beta-N-acetylglucosamine residue and another molecule. This activity is crucial in various biological processes, including:

1. **Glycoprotein and glycolipid degradation:** NAGases play a key role in the breakdown of complex carbohydrates attached to proteins and lipids. They remove terminal N-acetylglucosamine (GlcNAc) residues, contributing to the processing and degradation of these molecules.
2. **Lysosomal function:** NAGases are found in lysosomes, organelles responsible for the degradation of cellular debris and foreign materials. They contribute to the breakdown of glycoproteins and glycolipids, facilitating the recycling of cellular components.
3. **Immune response:** NAGases are involved in the immune response by modulating the activity of immune cells and influencing the presentation of antigens. They can degrade glycoconjugates on pathogens and immune cells, impacting their interactions and signaling.
4. **Cell signaling:** NAGases can influence cell signaling pathways by altering the glycosylation patterns of proteins involved in cell communication. They can remove GlcNAc residues from specific proteins, modulating their activity and downstream signaling events.
5. **Development and differentiation:** NAGases play a role in developmental processes by regulating the glycosylation of proteins involved in cell growth, differentiation, and morphogenesis.

The molecular function of NAGases involves the following key steps:

* **Substrate binding:** NAGases recognize and bind to the glycosidic bond between a GlcNAc residue and another molecule, often a sugar or an amino acid.
* **Catalytic mechanism:** The enzyme utilizes a catalytic mechanism that involves proton transfer, nucleophilic attack, and leaving group departure to break the glycosidic bond.
* **Product release:** The enzyme releases the cleaved GlcNAc residue and the modified substrate, enabling further processing or degradation.

Overall, beta-N-acetylglucosaminidase activity is essential for a wide range of cellular functions, including glycoprotein and glycolipid degradation, lysosomal function, immune response, cell signaling, and development.'
"

Proteins (1)

ProteinDefinitionTaxonomy
Protein O-GlcNAcaseA protein O-GlcNAcase that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60502]Homo sapiens (human)

Compounds (4)

CompoundDefinitionClassesRoles
2-acetamido-1,5-imino-1,2,5-trideoxy-d-glucitol2-acetamido-1,5-imino-1,2,5-trideoxy-D-glucitol: structure given in first source
n-acetylglucosamine thiazolineN-acetylglucosamine thiazoline: an analog of the oxazolinium bicyclic intermediate leading from N-acetylglucosamine to 1,6-anhydro-N-acetylmuramic acid
n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oximeN-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oxime: structure given in first source
thiamet g