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  Indian J Med Microbiol
 

Figure 2: Enzyme kinetic analysis of 4-MU glucuronidation in human liver microsomes catalyzed by UGT enzymes. Glucuronidation of 4-MU follows atypical enzyme kinetic model where the substrate itself act as an inhibitor after maximum velocity is achieved. Unlike the typical model of Michaelis–Menten kinetic, maximum velocity value in this model will never reach a plateau state when a high amount of substrates are introduced into the system. 4-MU: 4-methylumbelliferone; UGT: Uridine 5'-diphospho-glucuronosyltransferase

Figure 2: Enzyme kinetic analysis of 4-MU glucuronidation in human liver microsomes catalyzed by UGT enzymes. Glucuronidation of 4-MU follows atypical enzyme kinetic model where the substrate itself act as an inhibitor after maximum velocity is achieved. Unlike the typical model of Michaelis–Menten kinetic, maximum velocity value in this model will never reach a plateau state when a high amount of substrates are introduced into the system. 4-MU: 4-methylumbelliferone; UGT: Uridine 5'-diphospho-glucuronosyltransferase