A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.

@article{Schliebs1997ADM,
  title={A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.},
  author={Wolfgang Schliebs and Narmada Thanki and R. C. A. Jaenicke and Rik Wierenga},
  journal={Biochemistry},
  year={1997},
  volume={36 32},
  pages={9655-62}
}
Triosephosphate isomerase (TIM) is a very stable dimer. In order to understand better the importance of dimerization for stability and catalytic activity, we have constructed a monomeric double-mutation variant. The dimer interface residues Thr75 and Gly76, which are at the tip of loop 3, have been substituted by an arginine and a glutamate, respectively. In wild type TIM, these two residues are at a distance of 27 A from the active site (as measured within the same subunit). This new variant… CONTINUE READING

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