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

Author

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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)

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.

Suggested Citation

  • Shinya Fushinobu & Hiroshi Nishimasu & Daiki Hattori & Hyun-Jin Song & Takayoshi Wakagi, 2011. "Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase," Nature, Nature, vol. 478(7370), pages 538-541, October.
    • Handle: RePEc:nat:nature:v:478:y:2011:i:7370:d:10.1038_nature10457
    DOI: 10.1038/nature10457
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    Cited by:

    1. Dan Kozome & Adnan Sljoka & Paola Laurino, 2024. "Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Chongyang Wang & Changshui Liu & Xiaochuan Zhu & Quancai Peng & Qingjun Ma, 2023. "Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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