Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

Shinya Fushinobu, Hiroshi Nishimasu, Daiki Hattori, Hyun-Jin Song and Takayoshi Wakagi ()
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Shinya Fushinobu: Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku
Hiroshi Nishimasu: Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku
Daiki Hattori: Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku
Hyun-Jin Song: Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku
Takayoshi Wakagi: Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku

Nature, 2011, vol. 478, issue 7370, 538-541

Abstract: One active site, two activities The archaeal enzyme fructose 1,6-bisphosphate (FBP) aldolase/phosphatase catalyses two successive reactions in gluconeogenesis: an aldol condensation of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate to form FBP, and its subsequent hydrolysis to fructose-6-phosphate. Two groups present a series of structural snapshots of this novel bifunctional enzyme. The structures reveal a substantial remodelling of the active site that allows it to catalyse two highly dissimilar chemical reactions.

Date: 2011
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DOI: 10.1038/nature10457

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