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Figure 6 | BMC Biochemistry

Figure 6

From: Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A

Figure 6

Kinetic study of TraE, TraJ and TraK ATPase activity. ATP hydrolysis was monitored as a function of ATP concentration and kinetic parameters were calculated by Michealis-Menten plot. From vmax and KM values, it can be concluded that the ATP hydrolyzing activity of TraJ is higher than that of TraE and TraK. TraK has lower affinity for ATP as compared to TraE and TraJ. ATPase activity is given in nmol inorganic phosphate generated per min and per mg of the respective protein. The values are mean of three independent measurements.

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