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.
Cooper, S.J., Leonard, G.A., McSweeney, S.M., Thompson, A.W., Naismith, J.H., Qamar, S., Plater, A., Berry, A., Hunter, W.N.(1996) Structure 4: 1303-1315
- PubMed: 8939754 
- DOI: https://doi.org/10.1016/s0969-2126(96)00138-4
- Primary Citation of Related Structures:  
1ZEN - PubMed Abstract: 
[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 enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate. Structures are available for class I FBP-aldolases but there is a paucity of detail on the class II enzymes. Characterization is sought to enable a dissection of structure/activity relationships which may assist the construction of designed aldolases for use as biocatalysts in synthetic chemistry.
Organizational Affiliation: 
Department of Chemistry, University of Manchester, Oxford Road, Manchester, M13 9PL, UK. wnhunter@bad.dundee.ac.uk