Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family.
A new human liver UDP-glucuronosyltransferase (HlugP4) has been cloned and expressed in cell culture. The expressed enzyme has a molecular mass of 56 kDa and preferentially catalysed the glucuronidation of halogenated and bulky alkyl phenols. The C-terminal half of the sequence (246 amino acids) is 96% identical with the same portion of HlugP1, whereas the N-terminal half of the deduced protein sequences are only 38% identical. These results suggest that the two isoenzymes may be derived from the same gene by differential splicing of the gene product.
Wooster
R
R
Biochemical Medicine, University of Dundee, Ninewells Hospital and Medical School, Scotland, U.K.
Sutherland
L
L
Ebner
T
T
Clarke
D
D
Da Cruz e Silva
O
O
Burchell
B
B
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA; D014453:Glucuronosyltransferase / Q000235:genetics*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics*; D008099:Liver / Q000201:enzymology*; D008861:Microsomes; D008969:Molecular Sequence Data; D005810:Multigene Family
D007527:Isoenzymes; D004247:DNA; D014453:Glucuronosyltransferase