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Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase

Author

Listed:
  • Juan Du

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21)

  • Rafael F. Say

    (Lehrstuhl für Mikrobiologie, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1)

  • Wei Lü

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21)

  • Georg Fuchs

    (Lehrstuhl für Mikrobiologie, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1)

  • Oliver Einsle

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21
    BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-Universität Freiburg, Hebelstrasse 25)

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

  • Juan Du & Rafael F. Say & Wei Lü & Georg Fuchs & Oliver Einsle, 2011. "Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase," Nature, Nature, vol. 478(7370), pages 534-537, October.
    • Handle: RePEc:nat:nature:v:478:y:2011:i:7370:d:10.1038_nature10458
    DOI: 10.1038/nature10458
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    Cited by:

    1. 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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