1ZEN

CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE

Summary for 1ZEN

• Entry DOI: 10.2210/pdb1zen/pdb
• Descriptor: CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE, ZINC ION (3 entities in total)
• Functional Keywords: lyase, aldehyde, glycolysis
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 39190.78

Authors

Cooper, S.J.,Leonard, G.A.,Hunter, W.N. (deposition date: 1996-07-08, release date: 1997-07-07, Last modification date: 2024-02-14)

Primary citation

Cooper, S.J.,Leonard, G.A.,McSweeney, S.M.,Thompson, A.W.,Naismith, J.H.,Qamar, S.,Plater, A.,Berry, A.,Hunter, W.N.
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, 4:1303-1315, 1996

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.

PubMed: 8939754
DOI: 10.1016/S0969-2126(96)00138-4

Experimental method

X-RAY DIFFRACTION (2.5 Å)