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Figure 1 | BMC Biochemistry

Figure 1

From: Kinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa

Figure 1

Comparison of calculated and experimental kinetic data. The calculated and experimental normalised data for the PANAT-catalysed acetylation with the substrates AcCoA (A) and 5-aminosalicylic acid (B) is shown. The points represent the experimental data in three series: a = b (■), a = 1 ) and b = 1 (▲), expressed as the mean ± standard deviation of triplicate measurements. The lines represent values obtained through least-squares non-linear regression: a = b (long dashes), a = 1 (short dashes) and b = 1 (solid line). The values of the normalised substrate concentration constants A and B (eq. 1) were 0.4 and 0.2 mM respectively, and the normalised velocity is defined in equation 2. Both x- and y-coordinates are dimensionless. Reactions were performed in triplicate at 25°C and pH 8.0 as described in Methods.

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