The Human UDP Glucuronosyltransferase, UGT1A10, Glucuronidates Mycophenolic Acid
| Autor: | Peter I. Mackenzie, Behnaz Mojarrabi |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Signal peptide
DNA Complementary Molecular Sequence Data Biophysics Glucuronidation Biology Biochemistry Complementary DNA Animals Humans Amino Acid Sequence Cloning Molecular Glucuronosyltransferase Molecular Biology Peptide sequence chemistry.chemical_classification COS cells Molecular mass Cell Biology Mycophenolic Acid Molecular biology Enzyme chemistry COS Cells Microsomes Liver Microsome |
| Zdroj: | Biochemical and Biophysical Research Communications. 238:775-778 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.7388 |
| Popis: | The cDNA encoding the UDP glucuronosyltransferase, UGT1A10, has been cloned from human colon. The deduced amino acid sequence of the cDNA is 90% similar in sequence to that of a previously characterized form, UGT1A9 (Hlug P4), and contains a signal peptide and carboxyl-terminal hydrophobic domain characteristic of all UDP glucuronosyltransferases isolated to date. The enzyme synthesized in UGT1A10 cDNA-transfected COS-7 cells has a relative molecular mass of 56 kDa and is very active in the glucuronidation of mycophenolic acid (apparent Km of 34 microM and Vmax of 0.6 nmoles/min/mg protein). Other UGTs (UGT1A1, 1A3, 1A4, 1A6, 1A9, 2B7, 2B10 and 2B11) synthesized in COS cells had relatively little activity towards mycophenolic acid, suggesting that UGT1A10 may have a significant role in the elimination of this antineoplastic and immunosuppressive agent in vivo. |
| Databáze: | OpenAIRE |
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