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.
Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything
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H. Walden, G. Taylor, H. Lilie, T. Knura, R. Hensel; Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything. Biochem Soc Trans 1 April 2004; 32 (2): 305. doi: https://doi.org/10.1042/bst0320305
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