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

descriptionPublicationkeyboard_double_arrow_right Article 16 Jul 2019 English Publisher:Public Library of Science (PLoS)Journal:PLOS ONE, volume 14, page e0219664 (eissn: 1932-6203,

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Authors: Brian Torres; James S. Tyler; Kenneth A. Satyshur; Arnold E. Ruoho;

doi: 10.1371/journal.pone.0219664 , 10.5281/zenodo.3241882 , 10.5281/zenodo.3241881

pmid: 31310642

pmc: PMC6634407

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

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Abstract

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.

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Keywords

Models, Molecular, Protein Conformation, Science, Q, R, Methyltransferases, Sulfides, Crystallography, X-Ray, Methylation, Polymorphism, Single Nucleotide, Tryptamines, Isoenzymes, Kinetics, Organoselenium Compounds, Escherichia coli, Medicine, Humans, Disulfides, Alleles, Research Article

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