References

  1. Lebioda, L., Stec, B. Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Nature. 1988 Jun 16; 333(6174): 683-6.
  2. Lebioda, L., Stec, B., Brewer, J.M. The structure of yeast enolase at 2.25-Å resolution. An 8-fold beta + alpha barrel with a novel beta beta alpha alpha (beta alpha) 6 topology. J. Biol Chem. 1989 Mar 5; 264(7):3685-93.
  3. Lebioda, L., Stec, B., Brewer J.M., Tykarska, E. Inhibition of enolase: the crystal structures of enolase-Ca2+-2-phosphoglycerate and enolase-Zn2+-phosphoglycerate complexes at 2.2-Å resolution. Biochemistry. 1991 Mar 19; 30(11):2823-7.
  4. Lebioda, L., Stec, B. Mechanism of enolase: the crystal structure of enolase-Mg2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-Å resolution. Biochemistry. 1991 Mar 19; 30(11):2817-22.
  5. Stec, B., Lebioda, L. Refined structure of yeast apo-enolase at 2.25-Å resolution. J. Mol. Biol. 1990 Jan 5; 211(1):235-48.
  6. Zhang, E., Hatada, M., Brewer, J.M., Lebioda, L. Catalytic metal ion binding in enolase: the crystal structure of an enolase-Mn2+-phosphonoacetohydroxamate complex at 2.4-Å resolution. Biochemistry. 1994 May 24; 33(20):6295-6300.
  7. Zhang, E., Brewer, J.M., Minor, W., Carreira, L.A., Lebioda, L. Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0-Å resolution. Biochemistry. 1997 Oct 14; 36(41):12526-34.

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Updated: Friday, December 10, 1999
By Christina Golner
Chem 406: Biophysical Chemistry