title: Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything.
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.
authors.affiliation: Centre for Biomolecular Sciences, University of St Andrews, St Andrews, Fife KY16 9ST, Scotland, U.K.
authors.forename: H
authors.initials: H
authors.lastname: Walden
authors.forename: G
authors.initials: G
authors.lastname: Taylor
authors.forename: H
authors.initials: H
authors.lastname: Lilie
authors.forename: T
authors.initials: T
authors.lastname: Knura
authors.forename: R
authors.initials: R
authors.lastname: Hensel
mesh_terms: 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*
chemical_list: D005993:Glycerolphosphate Dehydrogenase; D014305:Triose-Phosphate Isomerase