Abstract
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 dinners. 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 oligornerization of the TtxTIM serves functional rather than stabilizing purposes.
| Original language | English |
|---|---|
| Pages (from-to) | 305-305 |
| Number of pages | 1 |
| Journal | Biochemical Society Transactions |
| Volume | 32 |
| Publication status | Published - Apr 2004 |
Keywords
- hyperthermophile
- thermostability
- triosephosphate isomerase
- MARITIMA
- PROTEINS
- TIM