EndoDglucuronidase

EndoDglucuronidase is not a widely standardized name for a specific enzyme in major biochemical databases. In some contexts the term may be used to refer to endo-acting enzymes that hydrolyze internal β-D-glucuronidic linkages, or it may be a variation of endo-β-D-glucuronidase or β-D-glucuronidase. Because nomenclature for glucuronidases is diverse, precise identification typically relies on substrate scope and assay data.

Endo-β-D-glucuronidases are generally considered glycoside hydrolases that cleave internal glycosidic bonds involving D-glucuronic acid residues within glucuronidated polymers. This endo-activity contrasts with exo-acting β-D-glucuronidases, which release terminal glucuronide units from substrates. The exact substrate range can vary among enzymes described as endo-acting, but common targets include glucuronidated polysaccharides or synthetic glucuronide-containing compounds used in biochemical assays.

Substrates for such activities may include glucuronidated polysaccharides, certain glycosaminoglycan fragments, and various glucuronide conjugates encountered in microbial metabolism or plant and tissue polysaccharides. In nature, reported examples come from diverse microorganisms that degrade glucuronidated materials to access carbon sources.

Applications of endo- or endo-acting glucuronidases include research on glucuronide bond cleavage in polysaccharides, studies of glycosaminoglycan degradation, and exploration of microbial drug metabolism where glucuronide conjugates are deconjugated. They can also aid in bioconversion or valorization of glucuronidated biomass in biotechnology contexts.

See also: beta-D-glucuronidase, endo-acting glycoside hydrolases, glycoside hydrolase families.