On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.

@article{Alber1981OnTT,
  title={On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.},
  author={Tom Alber and David W. Banner and Anne C. Bloomer and Gregory A. Petsko and David B. Phillips and P S Rivers and Ian A. Wilson},
  journal={Philosophical transactions of the Royal Society of London. Series B, Biological sciences},
  year={1981},
  volume={293 1063},
  pages={159-71}
}
Triose phosphate isomerase is a dimeric enzyme of molecular mass 56 000 which catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate. The crystal structure of the enzyme from chicken muscle has been determined at a resolution of 2.5 A, and an independent determination of the structure of the yeast enzyme has just… CONTINUE READING