Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure.

ABSTRACT: Structure-function relationships in the tetrameric enzyme urate oxidase were investigated using pressure perturbation. As the active sites are located at the interfaces between monomers, enzyme activity is directly related to the integrity of the tetramer. The effect of hydrostatic pressure on the enzyme was investigated by x-ray crystallography, small-angle x-ray scattering, and fluorescence spectroscopy. Enzymatic activity was also measured under pressure and after decompression. A global model, consistent with all measurements, discloses structural and functional details of the pressure-induced dissociation of the tetramer. Before dissociating, the pressurized protein adopts a conformational substate characterized by an expansion of its substrate binding pocket at the expense of a large

SUBMITTER: Girard E 

PROVIDER: S-EPMC2872268 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature