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. Author manuscript; available in PMC: 2011 Aug 10.
Published in final edited form as: Biochemistry. 2010 Aug 10;49(31):6715–6726. doi: 10.1021/bi1008744

Figure 5.

Figure 5

Substrate, pH, and detergent dependence of CcLpxI activity. Panel A. UDP-2,3-diacylglucosamine concentration dependence of CcLpxI activity under standard assay conditions. The apparent KM, fit using Kaleidograph, was 105 ± 25 μM; the apparent Vmax was 69 ± 5 μmols/min/mg. Panel B. CcLpxI activity as a function of pH. The activity is relatively constant at pH values between 6.5 and 9, but declines sharply below 6. Panel C. Effect of Triton X-100 concentration on the apparent specific activity of CcLpxI at 100 μM UDP-2,3-diacylglucosamine. Surface dilution kinetics are not apparent, and there is measurable activity in the absence of Triton.