期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 32, 期 -, 页码 305-305出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0320305
关键词
hyperthermophile; thermostability; triosephosphate isomerase
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.
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