Molecular Mechanism by which One Enzyme Catalyzes Two Reactions

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  • NISHIMASU Hiroshi
    Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
  • FUSHINOBU Shinya
    Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • WAKAGI Takayoshi
    Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo

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Other Title
  • 1つの酵素が2つの反応を触媒するしくみ
  • 1ツ ノ コウソ ガ 2ツ ノ ハンノウ オ ショクバイ スル シクミ

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Abstract

Unlike ordinary enzymes, fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) catalyzes two distinct reactions : (1) the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate to FBP, and (2) the dephosphorylation of FBP to fructose-6-phosphate. We solved the crystal structures of FBPA/P in complex with DHAP (its aldolase form) and FBP (its phosphatase form). The crystal structures revealed that FBPA/P exhibits the dual activities through a dramatic conformational change in the active-site architecture. Our findings expand the conventional concept that one enzyme catalyzes one reaction.

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