The inhibition of β-glucuronidase by saccharic acid and the role of the enzyme in glucuronide synthesis

Abstract

Hydrolysis of phenyl-glucuronide by beta-glucuronidase was strongly inhibited by saccharic acid. Closely related compounds were much less effective. Inhibition by saccharic acid was competitive, and a value of 6 x 10-5 [image] was obtained for Ki, the dissociation constant of the enzyme-inhibitor complex. Saccharic acid had no marked effect on synthesis of o-aminophenylglucuronide by mouse liver slices. Admn. of large doses of saccharic acid to mice did not influence liver regeneration after damage or growth in infant animals. No conjugation of o-aminophenol with glucuronic acid was observed after incubation in the presence of beta-glucuroni-dase.