Premium
Functional relevance of the internal hydrophobic cavity of urate oxidase
Author(s) -
Colloc'h Nathalie,
Prangé Thierry
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.03.017
Subject(s) - active site , hydrostatic pressure , chemistry , urate oxidase , tetramer , biophysics , stereochemistry , enzyme , biochemistry , thermodynamics , biology , physics
Urate oxidase from Aspergillus flavus is a 135 kDa homo‐tetramer which has a hydrophobic cavity buried within each monomer and located close to its active site. Crystallographic studies under moderate gas pressure and high hydrostatic pressure have shown that both gas presence and high pressure would rigidify the cavity leading to an inhibition of the catalytic activity. Analysis of the cavity volume variations and functional modifications suggest that the flexibility of the cavity would be an essential parameter for the active site efficiency. This cavity would act as a connecting vessel to give flexibility to the neighboring active site, and its expansion under pure oxygen pressure reveals that it might serve as a transient reservoir on its pathway to the active site.