In:
FEBS Letters, Wiley, Vol. 566, No. 1-3 ( 2004-05-21), p. 48-54
Abstract:
Oligomerization directs active site formation in homotrimeric 2 ′ ‐deoxyuridine triphosphate pyrophosphatases (dUTPases). Stability of the homotrimer is a central determinant in enzyme function. The present comparative studies of bacterial and fruitfly dUTPases with homologous 3D structures by differential scanning microcalorimetry; fluorescence, circular dichorism and infrared spectroscopies, demonstrate that unfolding is a two‐state highly cooperative transition in both dUTPases excluding a significantly populated intermediate state of dissociated and folded monomers. The eukaryotic protein is much less resistant against either thermal or guanidine hydrochloride‐induced denaturation. Results suggest that hydrophobic packing of the inner threefold channel of the dUTPase homotrimer greatly contributes to stability.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/j.febslet.2004.04.039
Language:
English
Publisher:
Wiley
Publication Date:
2004
detail.hit.zdb_id:
1460391-3
SSG:
12
Permalink
