Fig. 2: Enzymology and mutagenesis of recombinant mouse PTER in vitro. | Nature

Fig. 2: Enzymology and mutagenesis of recombinant mouse PTER in vitro.

From: PTER is a N-acetyltaurine hydrolase that regulates feeding and obesity

Fig. 2

a,b, Hydrolysis rates following incubation of purified recombinant mouse PTER (100 ng) and the indicated concentration of N-acetyltaurine (a) or 100 µM of the indicated substrates (b). Reactions were performed for 1 h at 37 °C. N = 3 per group. c, Molecular docking of mouse PTER and N-acetyltaurine. Individual amino acid residues, two zinc ions (dark blue) and one water molecule (light blue) are highlighted. d, N-acetyltaurine hydrolysis activity of total bacterial lysates overexpressing the indicated mouse PTER mutant (top) and western blot using an anti-6×His antibody (bottom). Reactions were performed with 100 µM N-acetyltaurine for 1 h at 37 °C. N = 3 per group. For a, b and d, data are shown as the mean ± s.e.m. Data were fitted to Michaelis–Menten kinetics (solid line) using GraphPad Prism. All experiments were repeated twice and similar results were obtained.

Source Data

Back to article page