Human erythrocyte membrane thiol methyltransferase. S-methylation of captopril, N-acetylcysteine, and 7 alpha-thio-spirolactone.

@article{Keith1984HumanEM,
  title={Human erythrocyte membrane thiol methyltransferase. S-methylation of captopril, N-acetylcysteine, and 7 alpha-thio-spirolactone.},
  author={Richard Alan Keith and Ian Jardine and Adrian L Kerremans and Richard M. Weinshilboum},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={1984},
  volume={12 6},
  pages={
          717-24
        }
}
Thiol methylation is an important pathway in the biotransformation of sulfhydryl drugs such as captopril. Human red blood cell (RBC) membranes contain a thiol methyltransferase (TMT) activity that catalyzes the S-methylation of 2-mercaptoethanol (2-ME). These experiments were performed to determine whether human RBC membranes contained enzymes that could catalyze the S-methylation of thiol drugs, and, if so, to determine whether those enzymes were similar to the RBC membrane TMT that catalyzes… CONTINUE READING