Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.

@article{Dalby1999CrystalSO,
  title={Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.},
  author={Andrew R. Dalby and Zbigniew Dauter and Jennifer A. Littlechild},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 2},
  pages={291-7}
}
Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Catalysis involves the formation of a Schiff's base intermediate formed at the epsilon-amino group of Lys229. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved… CONTINUE READING

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