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Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum

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  • Sangwoo Kim

    (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University
    School of Nano-Bioscience and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST))

  • Yu-Sin Jang

    (KAIST)

  • Sung-Chul Ha

    (Pohang Accelerator Laboratory, Pohang University of Science and Technology)

  • Jae-Woo Ahn

    (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University)

  • Eun-Jung Kim

    (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University)

  • Jae Hong Lim

    (Pohang Accelerator Laboratory, Pohang University of Science and Technology)

  • Changhee Cho

    (KAIST)

  • Yong Shin Ryu

    (School of Nano-Bioscience and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST))

  • Sung Kuk Lee

    (School of Nano-Bioscience and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST))

  • Sang Yup Lee

    (KAIST
    Center for Systems and Synthetic Biotechnology, Institute for the BioCentury, and Bioinformatics Research Center, KAIST)

  • Kyung-Jin Kim

    (School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University)

Abstract

Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch modulation through reversible disulfide bond formation between two catalytic cysteine residues, Cys88 and Cys378. When CaTHL is overexpressed in wild-type C. acetobutylicum, butanol production is reduced due to the disturbance of acidogenic to solventogenic shift. The CaTHLV77Q/N153Y/A286K mutant, which is not able to form disulfide bonds, exhibits higher activity than wild-type CaTHL, and enhances butanol production upon overexpression. On the basis of these results, we suggest that CaTHL functions as a key enzyme in the regulation of the main metabolism of C. acetobutylicum through a redox-switch regulatory mechanism.

Suggested Citation

  • Sangwoo Kim & Yu-Sin Jang & Sung-Chul Ha & Jae-Woo Ahn & Eun-Jung Kim & Jae Hong Lim & Changhee Cho & Yong Shin Ryu & Sung Kuk Lee & Sang Yup Lee & Kyung-Jin Kim, 2015. "Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum," Nature Communications, Nature, vol. 6(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9410
    DOI: 10.1038/ncomms9410
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