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Alpha-L-arabinofuranosidases (EC 3.2.1.55) are exo-acting glycoside hydrolases that catalyze the hydrolysis of terminal non-reducing alpha-L-arabinofuranosyl residues from various oligosaccharides and polysaccharides (UniProt, 2024). These enzymes are predominantly found in bacteria, fungi, and plants, where they play a crucial role in the degradation of hemicellulose and pectin, which are major components of the plant cell wall (CAZy Database, 2024). In a therapeutic context, they are not typical human drug targets but are extensively studied for use in Antibody-Directed Enzyme Prodrug Therapy (ADEPT) (PubMed, PMID: 10861325). In ADEPT, a microbial alpha-L-arabinofuranosidase is conjugated to a tumor-specific antibody to locally activate a non-toxic prodrug into a potent cytotoxic agent at the site of a tumor. Additionally, these enzymes are vital in industrial processes such as the production of biofuels, the clarification of fruit juices, and the enhancement of aromas in winemaking (Journal of Applied Microbiology, 2021). Because they are of microbial origin, their use in humans is associated with significant safety concerns, primarily the risk of immunogenicity and potential hypersensitivity reactions.
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinofuranosides
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