Figure 11.

Identification of regions on the surface of TPI relevant for kcat/Km and Km kinetic parameters. By scanning patches and residues on the protein surface, calculating the correlation between electrostatic potential differences and the respective kinetic parameters kcat/Km (a) and Km (b) at each position, different regions on the TPI protein surface were found to give the best correlations with experimental data. Regions where variations in the electrostatic potential are best correlated with variations in kcat/Km (a) and Km (b) (see text for details). (c) ribbon presentation of the TPI monomer with important residues shown: the flexible loop is in magenta (W168-T175), the catalytic residues Glu165 and His95, as well as the conserved Lys13 important for electrostatic steering of the substrate are shown in red. The centers of the regions selected for correlating Km and kcat/Km parameters are shown by red balls, on the left – W168CZ3 and on the right – L230O. (d): electrostatic potential conservation: red: highest to blue: lowest.

Gabdoulline et al. BMC Bioinformatics 2007 8:373   doi:10.1186/1471-2105-8-373
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