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. 2016 Apr;22(4):518–529. doi: 10.1261/rna.055152.115

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© 2016 Ziemniak et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 4. — Single-turnover inhibition kinetics of 12b with SpDcp1/2 and a 29-nt native-capped RNA substrate. (A) Fits to determine K_M^app and k_max at different inhibitor concentrations; K_M^app increases by fivefold and k_max decreases by threefold in the presence of 1 mM inhibitor, demonstrating that 12b is a mixed inhibitor of Dcp1/2 (see Supplemental Table S1). (B) Fits to Equation 1 of normalized rate data versus inhibitor concentration to determine K_I under subsaturating enzyme concentrations. (C) Bar graph of determined K_I values for 12b with Dcp1/2 or Dcp2 and m⁷GpppG with Dcp1/2; nucleotide 12b binds with ∼20-fold tighter affinity than m⁷GpppG.