Fig. 2: Determination of inhibition constants for  β-lactamases. | Nature Communications

Fig. 2: Determination of inhibition constants for  β-lactamases.

From: An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes

Fig. 2: Determination of inhibition constants for  β-lactamases.

Inhibition constants (Ki) for BLIP with a CTX-M-15 wild type, b CTX-M-15 N106S, c CTX-M-14 wild type, d CTX-M-14 N106S, e CTX-M-15 V133T, and f CTX-M-15 G240D β-lactamases. BLIP concentrations are indicated on the X-axis and the initial velocity of nitrocefin hydrolysis in the presence of BLIP divided by the velocity in the absence of BLIP is shown on Y-axis. The initial velocities shown are the mean of at least two determinations with the associated error bar indicating the standard deviation of the value. Values for Ki were determined by fitting to the Morrison equation (Methods). The error on the Ki value is the standard error based on the fitting to the equation. Source data are provided as Source data file.

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