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

Juan Du, Rafael F. Say, Wei Lü, Georg Fuchs and Oliver Einsle ()
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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

Nature, 2011, vol. 478, issue 7370, 534-537

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/nature10458

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