Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Colloc'h N,Prangé Tdoi
10.1016/j.febslet.2014.03.017subject
Has Abstractpub_date
2014-05-02 00:00:00pages
1715-9issue
9eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00222-1journal_volume
588pub_type
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