Molecular cloning and functional characterization of the cDNA encoding the murine thiopurine S-methyltransferase (TPMT).
Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines. Here we report the isolation and functional characterization of the murine TPMT cDNA. The screening of expressed sequence tags database led to isolation of a murine cDNA clone containing an uninterrupted ORF encoding the protein with an amino acid sequence that is 82% similar and 78% identical to the human TPMT. The expression product of the murine cDNA in rabbit reticulocyte and wheat germ lysate coupled transcription-translation systems showed TPMT enzymatic activity. We conclude that the isolated cDNA clone represents the murine TPMT cDNA.
Fessing
M Y
MY
Department of Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Belkov
V M
VM
Krynetski
E Y
EY
Evans
W E
WE
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000302:isolation & purification; D006801:Humans; D008780:Methyltransferases / Q000235:genetics* / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011817:Rabbits; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D011994:Recombinant Proteins; D008780:Methyltransferases; C022745:thiopurine methyltransferase