Title |
Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum
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Published in |
Nature Communications, September 2015
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DOI | 10.1038/ncomms9410 |
Pubmed ID | |
Authors |
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 |
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 CaTHL(V77Q/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. |
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