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Figure 6 | BMC Structural Biology

Figure 6

From: Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties

Figure 6

Kinetic analysis of the thermostability of wild-type and mutant EstE1. The enzymes (6.0 μM) of wild-type EstE1 (), EstE1F276A (■), EstE1F276E (□), EstE1V274A (▲), EstE1V274A/F276A (), EstE1L299D (), EstE1R270A (), EstE1E295A (), and EstE1R270A/E295A (), in 20 mM potassium phosphate buffer (pH 7.0) were incubated at 80°C for the indicated times. Residual activities were then determined by measuring the amount of p-nitrophenol released by esterase-catalyzed hydrolysis. The activity of a non-incubated sample was defined as 100%

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