Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything.
The triosephosphate isomerase of the hyperthermophilic crenarchaeum Thermoproteus tenax (TtxTIM) represents a homomeric tetramer. Unlike the triosephosphate isomerases of other hyperthermophiles, however, the association of the TtxTIM tetramers is looser, allowing a reversible dissociation into inactive dimers. The dimer/tetramer equilibrium of TtxTIM is shifted to the tetrameric state through a specific interaction with glycerol-1-phosphate dehydrogenase of T. tenax, suggesting that higher oligomerization of the TtxTIM serves functional rather than stabilizing purposes.
Walden
H
H
Centre for Biomolecular Sciences, University of St Andrews, St Andrews, Fife KY16 9ST, Scotland, U.K.
Taylor
G
G
Lilie
H
H
Knura
T
T
Hensel
R
R
D019281:Dimerization; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006358:Hot Temperature; D011485:Protein Binding; D011489:Protein Denaturation; D041542:Thermoproteus / Q000201:enzymology*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*
D005993:Glycerolphosphate Dehydrogenase; D014305:Triose-Phosphate Isomerase