Microbial glycoside hydrolase (GH) (GH)

Microbial glycoside hydrolases (GHs) are a vast and diverse family of enzymes responsible for the hydrolysis of glycosidic bonds in complex carbohydrates and glycoconjugates. These enzymes are essential for various biological processes in bacteria, fungi, and archaea, including the degradation of biomass for energy, the remodeling of the microbial cell wall, and the modification of host cell surfaces during infection (Lombard et al., 2014, Nucleic Acids Res). In the human gut, microbial GHs are pivotal for breaking down non-digestible dietary polysaccharides, thereby influencing host metabolism and immune function (Koropatkin et al., 2012, Nat Rev Microbiol). As therapeutic targets, they are exploited in the treatment of metabolic disorders, such as type 2 diabetes, where drugs like acarbose inhibit microbial and human alpha-glucosidases to reduce postprandial glucose spikes (Balfour & McTavish, 1993, Drugs). Furthermore, GHs are targeted in anti-infective strategies to disrupt biofilm stability or prevent the attachment of pathogens to host tissues (Fleming & Rumbaugh, 2017, Microorganisms). The development of selective inhibitors remains a primary challenge due to the structural conservation between certain microbial GHs and their human counterparts, which can lead to off-target gastrointestinal effects (Withers, 2001, Carbohydr Polym).

Other names

GlycosidaseO-glycosyl hydrolaseCarbohydrate-active enzymeCAZymeGlycosyl hydrolase

Competitive or irreversible inhibition of the enzyme's active site, preventing the cleavage of glycosidic bonds in polysaccharides, glycoproteins, or glycolipids.