Fluoride inhibition of enolase: crystal structure and thermodynamics.

@article{Qin2006FluorideIO,
  title={Fluoride inhibition of enolase: crystal structure and thermodynamics.},
  author={Jie Qin and Geqing Chai and John M. Brewer and Leslie L. Lovelace and Lukasz Lebioda},
  journal={Biochemistry},
  year={2006},
  volume={45 3},
  pages={
          793-800
        }
}
Enolase is a dimeric metal-activated metalloenzyme which uses two magnesium ions per subunit: the strongly bound conformational ion and the catalytic ion that binds to the enzyme-substrate complex inducing catalysis. The crystal structure of the human neuronal enolase-Mg2F2P(i) complex (enolase fluoride/phosphate inhibitory complex, EFPIC) determined at 1.36 A resolution shows that the combination of anions effectively mimics an intermediate state in catalysis. The phosphate ion binds in the… Expand
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