Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum

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 () and Kyung-Jin Kim ()
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Sangwoo Kim: School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University
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
Kyung-Jin Kim: School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms9410

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