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Published on: February 17, 2017
Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything
1Centre for Biomolecular Sciences, University of St Andrews, St Andrews, Fife KY16 9ST, Scotland, U.K.
Abstract:
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.
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