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Carbohydrate-active enzymes (CAZymes) are a large and diverse class of enzymes responsible for the synthesis, modification, and catabolism of complex carbohydrates and glycoconjugates (Lombard et al., 2014). They are organized into functional families based on amino acid sequence similarity, including glycoside hydrolases (GHs), glycosyltransferases (GTs), polysaccharide lyases (PLs), and carbohydrate esterases (CEs) (Drula et al., 2022). These enzymes play fundamental roles in biological processes such as energy production, the structural integrity of cell walls, and the complex glycosylation of proteins and lipids essential for cell signaling and immune recognition (Cantarel et al., 2009). In clinical practice, CAZymes are major therapeutic targets; for example, alpha-glucosidase inhibitors are used to manage type 2 diabetes by slowing carbohydrate digestion, while neuraminidase inhibitors are critical for treating influenza by blocking the release of viral progeny (Davies & Henrissat, 1995). Furthermore, genetic deficiencies in specific CAZymes lead to lysosomal storage diseases, which are addressed through enzyme replacement or substrate reduction therapies (Henrissat, 1991). Because the term refers to a broad category of thousands of distinct enzymes rather than a single molecular entity, it is typically used as a classification framework in genomics and biotechnology (Lombard et al., 2014).
Competitive inhibition of glycoside hydrolases to delay glucose absorption; inhibition of viral neuraminidase to prevent pathogen release; substrate reduction therapy by inhibiting glycosyltransferases; enzyme replacement therapy to restore deficient hydrolytic activity.
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