Published June 8, 2019
| Version v1
Journal article
Open
Human indole(ethyl)amine-N-methyltransferase (hINMT) catalyzed methylation of tryptamine dimethylsulfide and dimethylselenide is enhanced under reducing conditions - a comparison between 254C and 254F, two common hINMT variants
Authors/Creators
- 1. Department of Neuroscience, School of Medicine and Public Health, University of Wisconsin, Madison
- 2. Small Molecule Screening Facility, Carbone Cancer Center, School of Medicine and Public Health, University of Wisconsin, Madison
Description
This research article details data to show that the enzymatic activity of the 254C SNP of human indole(ethyl)amine-N-methyltransferase (hINMT) was significantly affected by the presence or absence of reducing agent in vitro. A common variant, 254F, eliminated sensitivity to this variable for tryptamine and DMS. A 44C/254C redox sensitive disulfide bond in hINMT is proposed.
This research article details data to show that hINMT has significant thioether-S-methyltransferase activity and showed a more favorable Km for dimethylselenide than tryptamine in vitro in the presence of the reducing agent DTT.