Glucuronidase β [MD432]

Glucuronidases β are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates. Human β-glucuronidase is a type of glucuronidase that catalyzes hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides as heparan sulfate. Beta-glucuronidase plays a crucial role in glucuronide hydrolysis, supporting detoxification and excretion of endogenous and exogenous compounds. Glucuronidases β deficiencies cause mucopolysaccharidosis type VII, a lysosomal storage disorder marked by glycosaminoglycan buildup, resulting in severe physiological effects. Beta-glucuronidase forms a homotetramer, with each subunit containing a jelly roll barrel, an immunoglobulin constant domain, and a TIM barrel essential for catalytic function. Glu 451 and Glu 540 residues are critical for enzymatic activity, and mutations at these sites can disrupt structure and function. Beta-glucuronidase regulation influences tumorigenesis and cancer invasiveness, making beta-glucuronidase a potential therapeutic target.