Kinetic caspase-6 enzymatic studies with compound 3 show uncompetitive mechanism of inhibition with (VEID)₂R110 substrate.

<p>(A) The initial enzyme velocity of caspase-6 was plotted against the indicated concentration of (VEID)₂R110 substrate in the presence of 0 nM (DMSO-black), 3 nM (red), 10 nM (orange), 30 nM (green) or 100 nM (blue) compound <b>3</b>. Double reciprocal plot of this data can be found in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050864#pone.0050864.s001" target="_blank">Figure S1</a> and Michaelis-Menten constants can be found in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050864#pone.0050864.s006" target="_blank">Table S3</a>. (B) Concentration-response analysis of compound <b>3</b> when tested in the presence of 0.5 µM (red), 5 µM (black) or 20 µM (blue) (VEID)₂R110 substrate. Michaelis-Menten kinetic experiments were performed with single points while concentration-response curves were performed in duplicate. Each data set represents 1 of at least 3 experiments with similar results.