Crystal structure of a trapped phosphoenzyme during a catalytic reaction
The crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water.
Publication Source (Journal or Book title)
Nature Structural Biology
Lee, Y., Olson, T., Ogata, C., Levitt, D., Banaszak, L., & Lange, A. (1997). Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nature Structural Biology, 4 (8), 615-618. https://doi.org/10.1038/nsb0897-615