The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.

@article{Cooper1996TheCS,
  title={The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.},
  author={Stephanie J. Cooper and Gordon A. Leonard and Se{\'a}n M. McSweeney and Andrew William Thompson and James H. Naismith and Seema S Qamar and Andy Plater and Alan Berry and William N. Hunter},
  journal={Structure},
  year={1996},
  volume={4 11},
  pages={1303-15}
}
BACKGROUND [corrected] Aldolases catalyze a variety of condensation and cleavage reactions, with exquisite control on the stereochemistry. These enzymes, therefore, are attractive catalysts for synthetic chemistry. There are two classes of aldolase: class I aldolases utilize Schiff base formation with an active-site lysine whilst class II enzymes require a divalent metal ion, in particular zinc. Fructose-1,6-bisphosphate aldolase (FBP-aldolase) is used in gluconeogenesis and glycolysis; the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

Similar Papers

Loading similar papers…