PMID:8939754
| Citation |
Cooper, SJ, Leonard, GA, McSweeney, SM, Thompson, AW, Naismith, JH, Qamar, S, Plater, A, Berry, A and Hunter, WN (1996) 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. Structure 4:1303-15 |
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| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cations/chemistry; Computer Simulation; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Escherichia coli Proteins; Fructose-Bisphosphate Aldolase/chemistry; Fructose-Bisphosphate Aldolase/classification; Metalloproteins/chemistry; Metalloproteins/classification; Models, Molecular; Molecular Sequence Data; Potassium/chemistry; Protein Conformation; Protein Structure, Secondary; Zinc/chemistry |
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