| First Author | Warner DR | Year | 1995 |
| Journal | Biochim Biophys Acta | Volume | 1246 |
| Issue | 2 | Pages | 160-6 |
| PubMed ID | 7819283 | Mgi Jnum | J:22541 |
| Mgi Id | MGI:70404 | Doi | 10.1016/0167-4838(94)00186-k |
| Citation | Warner DR, et al. (1995) Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase. Biochim Biophys Acta 1246(2):160-6 |
| abstractText | Thioether S-methyltransferase catalyzes transfer of the methyl group from S-adenosylmethionine to X in compounds of the structure R-X-R', where X may be sulfur, selenium, or tellurium, and R and R' may be various organic groups. To obtain a cDNA clone of thioether S-methyltransferase, a mouse lung cDNA library in lambda gt11 was screened with a 99 base-pair probe obtained by performing the polymerase chain reaction on oligo(dT) primed, reverse transcribed, mouse lung RNA using two degenerate primers designed from partial amino-acid sequences of the enzyme. The entire coding and 3'-untranslated regions were obtained and sequenced. The predicted protein contains 264 amino-acid residues and has a calculated M(r) of 29,460. The amino-acid sequence of thioether S-methyltransferase contains three motifs characteristic of many methyltransferases and has a high level of identity with the amino-acid sequences of nicotinamide N-methyltransferase and phenylethanolamine N-methyltransferase. However, in spite of the fact that they are both mammalian cytosolic sulfur methyltransferases, the sequences of thioether S-methyltransferase and thiopurine S-methyltransferase share little identity. |
