Thiol S-methyltransferase

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In enzymology, a thiol S-methyltransferase (EC 2.1.1.9) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + a thiol $\rightleftharpoons$ S-adenosyl-L-homocysteine + a thioether

Thus, the two substrates of this enzyme are S-adenosyl methionine and thiol, whereas its two products are S-adenosylhomocysteine and thioether.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:thiol S-methyltransferase. Other names in common use include S-methyltransferase, thiol methyltransferase, and TMT. This enzyme participates in selenoamino acid metabolism.

[edit] References

IUBMB entry for 2.1.1.9
BRENDA references for 2.1.1.9 (Recommended.)
PubMed references for 2.1.1.9
PubMed Central references for 2.1.1.9
Google Scholar references for 2.1.1.9
Borchardt RT, Cheng CF (1978). "Purification and characterization of rat liver microsomal thiol methyltransferase". Biochim. Biophys. Acta. 522: 340–53. PMID 623768.
Bremer J and Greenberg DM (1961). "Enzymic methylation of foreign sulfhydryl compounds". Biochim. Biophys. Acta 46: 217–224. doi:10.1016/0006-3002(61)90746-6.
Weisiger RA, Jakoby WB (1979). "Thiol S-methyltransferase from rat liver". Arch. Biochem. Biophys. 196: 631–7. doi:10.1016/0003-9861(79)90317-5. PMID 485170.