Abstract Cyanobacterial fructose-1,6/sedoheptulose-1,7-bisphosphatase (cy-FBP/SBPase) plays a vital role in gluconeogenesis and in photosynthetic carbon reduction pathway and is thus a potential enzymatic target for inhibition of harmful cyanobacterial blooms or weed or fungi. We crystallized and determined the structure of cy-FBP/SBPase complex. The results provide new insight into the molecular mechanisms of structure and catalysis of cy-FBP/SBPase. Then a series of novel hit compounds were selected and synthesized by using a pharmacophore-based and ligand structure-based designing and screening strategy. The possible interaction of the residues with inhibitors provided insight into the binding-mode between the inhibitors and substrate binding pocket. Our modeling strategies and screening methods employed are appropriate for searching novel lead compounds having both structural diversity and high inhibitory activity against cy-FBP/SBPase. Our studies provide novel insight into the evolution of this enzyme family and may help in the design of inhibitors as algicide or herbicide or fungicide. Shown in the figures are a crystal structure of cy-FBP/SBPase+AMP+FBP and the potential binding mode of hit compound with cy-FBP/SBPase

Structure and inhibitor screening of cyanobacterial fructose-1,6/sedoheptulose-1,7-bisphosphatase

248th National Meeting (2014)

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