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. 2014 Apr 14;53(18):2956–2965. doi: 10.1021/bi500175p

Figure 2.

Figure 2

Selectivity profile of PDAT for N-methyltransferases. (A) Inhibition of rabINMT by PDAT. Data are presented as a percentage of the control after background subtraction, and the absence of PDAT was normalized as 100%. (B) Inhibition of hINMT by PDAT. hINMT assays were conducted with tryptamine as a substrate and [14C]SAM as the methyl donor, in the absence or presence of 2 mM PDAT. (C) Lack of inhibition of human recombinant PNMT by PDAT. PNMT assays were conducted like hINMT assays but with phenylethanolamine (PEA) as a substrate. (D) Lack of PDAT inhibition of hNNMT. hNNMT assays were conducted as described for hINMT assays but using nicotinamide as a substrate.