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Since only studies on human enzyme are likely to be of value …


Biology Articles » Biochemistry » Sugar recognition by human galactokinase » Figures

Figures
- Sugar recognition by human galactokinase

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Figure 1. The structure of the galactose and phosphate binding sites from L. lactis galactokinase [14]. The protein was crystallised in the presence of both galactose and inorganic phosphate (both shown with yellow bonds). The following colour scheme has been used for the atoms: Carbon = black, Oxygen = red, Nitrogen = blue, Phosphate = pink. Distances of less than 0.32 nm are shown as dashed lines. Figure courtesy of Hazel Holden (University of Wisconsin).

Figure 1

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 Figure 2. The structures of the sugars used in this investigation.

Figure 2

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Figure 3. 2-deoxy-D-galactose (2dG) is a substrate for human galactokinase. Steady state kinetic analysis was carried out as described in Materials and Methods. Each kcat,app value is derived, using non-linear curve-fitting [25], from a set of rates data at a single sub-saturating substrate concentration. Error bars represent the standard error in kcat,app as derived by from the fitting process. The lines are non-linear curve fits of the kcat,app data to the equation kcat,app = kcat[substrate]/(Km + [substrate]). The following parameters were derived from this fitting: kcat = 4.8 ± 0.3 s-1; Km,ATP = 59 ± 9 μM; Km,2dG = 1100 ± 110 μM; kcat/Km,ATP = (8.1 ± 0.8) × 104 l.mol-1.s-1; kcat/Km,2dG = 4200 ± 270 l.mol-1.s-1.

Figure 3

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Figure 4. Kinetic analysis of the soluble mutants, E43A and E43G. Error bars represent the standard error as derived from the non-linear curve fitting (see materials and methods). The kinetic parameters derived from these curve fits are detailed in table 1.

Figure 4

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Source: BMC Biochemistry 2003, 4:16

 

  

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