Substrate specificity of the human UDP‐glucuronosyltransferase UGT2B4 and UGT2B7
@article{Barr2007SubstrateSO, title={Substrate specificity of the human UDP‐glucuronosyltransferase UGT2B4 and UGT2B7}, author={L. Barr{\'e} and S. Fournel-Gigleux and M. Finel and P. Netter and J. Magdalou and M. Ouzzine}, journal={The FEBS Journal}, year={2007}, volume={274} }
The human UDP‐glucuronosyltransferase (UGT) isoforms UGT2B4 and UGT2B7 play a major role in the detoxification of bile acids, steroids and phenols. These two isoforms present distinct but overlapping substrate specificity, sharing common substrates such as the bile acid hyodeoxycholic acid (HDCA) and catechol‐estrogens. Here, we show that in UGT2B4, substitution of phenylalanine 33 by leucine suppressed the activity towards HDCA, and impaired the glucuronidation of several substrates, including… Expand
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References
SHOWING 1-10 OF 22 REFERENCES
Alteration of human UDP-glucuronosyltransferase UGT2B17 regio-specificity by a single amino acid substitution.
- Biology, Medicine
- Journal of molecular biology
- 1999
- 33
Structural and functional studies of UDP-glucuronosyltransferases.
- Chemistry, Medicine
- Drug metabolism reviews
- 1999
- 458
Expression and Characterization of Recombinant Human UDP-glucuronosyltransferases (UGTs)
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 2003
- 141
- PDF
Novel Functional Polymorphisms in the UGT1A7 and UGT1A9 Glucuronidating Enzymes in Caucasian and African-American Subjects and Their Impact on the Metabolism of 7-Ethyl-10-hydroxycamptothecin and Flavopiridol Anticancer Drugs
- Biology, Medicine
- Journal of Pharmacology and Experimental Therapeutics
- 2003
- 195
- PDF
The regio- and stereo-selectivity of C19 and C21 hydroxysteroid glucuronidation by UGT2B7 and UGT2B11.
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1997
- 73
Opioids bind to the amino acids 84 to 118 of UDP-glucuronosyltransferase UGT2B7.
- Chemistry, Medicine
- Molecular pharmacology
- 2003
- 28
The interactions between the N-terminal and C-terminal domains of the human UDP-glucuronosyltransferases are partly isoform-specific, and may involve both monomers.
- Chemistry, Medicine
- Biochemical pharmacology
- 2004
- 44
Human UDP-glucuronosyltransferases: metabolism, expression, and disease.
- Biology, Medicine
- Annual review of pharmacology and toxicology
- 2000
- 1,381
Expression and Functional Domains of Rabbit Liver UDP-glucuronosyltransferase 2B16 and 2B13*
- Biology, Medicine
- The Journal of Biological Chemistry
- 1997
- 25
- PDF