The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid

Biochem Biophys Res Commun. 1997 Sep 29;238(3):775-8. doi: 10.1006/bbrc.1997.7388.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cloning, Molecular
  • DNA, Complementary / isolation & purification
  • Glucuronosyltransferase / genetics
  • Glucuronosyltransferase / metabolism*
  • Humans
  • Microsomes, Liver / enzymology
  • Molecular Sequence Data
  • Mycophenolic Acid / metabolism*


  • DNA, Complementary
  • Glucuronosyltransferase
  • Mycophenolic Acid

Associated data

  • GENBANK/U39550