Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.

@article{Williams1999StructuralAM,
  title={Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.},
  author={Julian C. Williams and J. Ph. Zeelen and Gitte Neubauer and Gert Vriend and Jan Backmann and Paul A. M. Michels and Anne Marie Lambeir and Rik Wierenga},
  journal={Protein engineering},
  year={1999},
  volume={12 3},
  pages={243-50}
}
The dimeric enzyme triosephosphate isomerase (TIM) has a very tight and rigid dimer interface. At this interface a critical hydrogen bond is formed between the main chain oxygen atom of the catalytic residue Lys13 and the completely buried side chain of Gln65 (of the same subunit). The sequence of Leishmania mexicana TIM, closely related to Trypanosoma brucei TIM (68% sequence identity), shows that this highly conserved glutamine has been replaced by a glutamate. Therefore, the 1.8 A crystal… CONTINUE READING

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