Article
The interactions between the N-terminal and C-terminal domains of the human UDP-glucuronosyltransferases are partly isoform-specific, and may involve both monomers.
Biochemical pharmacology - 15 Dec 2004
Kurkela Mika, Hirvonen Jouni, Kostiainen Risto, Finel Moshe
Abstract excerpt
The pathological mutation Y486D was previously shown to reduce the activities of the UDP-glucuronosyltransferases (UGTs) 1A1 and 1A6 by about 88% and 99%, respectively. Surprisingly, the corresponding mutation in UGT1A9 (Y483D) doubled the Vmax of scopoletin glucuronidation, whereas the entacapone glucuronidation rate was decreased by about 50%. Due to the primary structure identity of the C-terminal half of all...
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