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FrsA functions as a cofactor-independent decarboxylase to control metabolic flux

Nature Chemical Biology volume 7, pages 434–436 (2011)Cite this article

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Abstract

The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIAGlc increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIAGlc (d-IIAGlc). Crystal structures of FrsA and its complex with d-IIAGlc revealed residues required for catalysis as well as the structural basis for the activation by d-IIAGlc.

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Figure 1: Enzymatic activity of FrsA.
Figure 2: Structures of FrsA and the FrsA–d-IIAGlc complex.

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Acknowledgements

We are grateful to Y.-J. Lee, H.-S. Lee, S.J. Chung and J.K. Lee for comments on the manuscript. This work was supported by the Marine and Extreme Genome Research Center program of Ministry of Land, Transport and Maritime Affairs, the Mid-career Researcher Program through National Research Foundation grant funded by the Ministry of Education, Science and Technology (2009-0092822), a KORDI in-house program (PE98513) and the Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of Ministry of Land, Transport and Maritime Affairs.

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Author notes

  1. Kyung-Jo Lee and Chang-Sook Jeong: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Environmental Science, Hankuk University of Foreign Studies, Yongin, Republic of Korea

    Kyung-Jo Lee, Hyun-Jung Lee & Kyu-Ho Lee

  2. Marine Biotechnology Research Center, Korea Ocean Research & Development Institute (KORDI), Ansan, Republic of Korea

    Chang-Sook Jeong, Young Jun An, Jung-Hyun Lee & Sun-Shin Cha

  3. Department of Environmental Medical Biology and Institute of Tropical Medicine, The Brain Korea 21 Project, Yonsei University College of Medicine, Seoul, Republic of Korea

    Soon-Jung Park

  4. Department of Biophysics and Chemical Biology, Seoul National University, Seoul, Republic of Korea

    Yeong-Jae Seok

  5. Department of Biotechnology, The Catholic University of Korea, Bucheon, Republic of Korea

    Pil Kim

  6. Department of Marine Biotechnology, University of Science and Technology, Daejeon, Republic of Korea

    Jung-Hyun Lee & Sun-Shin Cha

Authors
  1. Kyung-Jo Lee
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Contributions

S.-S.C. and K.-H.L. designed the project, analyzed data and wrote the manuscript. K.-J.L., C.-S.J., Y.J.A., H.-J.L., S.-J.P. and S.-S.C. performed experiments. Y.-J.S. gave advice on the design of this project and the NMR experiments. P.K. gave advice on the biochemical experiments. J.-H.L. contributed analytic tools.

Corresponding authors

Correspondence to Kyu-Ho Lee or Sun-Shin Cha.

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The authors declare no competing financial interests.

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Lee, KJ., Jeong, CS., An, Y. et al. FrsA functions as a cofactor-independent decarboxylase to control metabolic flux. Nat Chem Biol 7, 434–436 (2011). https://doi.org/10.1038/nchembio.589

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