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Lee, Sung Kuk
Synthetic Biology & Metabolic Engineering Laboratory
Research Interests
  • Biofuels production
  • Gene discovery
  • Protein engineering
  • Development of gene expression systems
  • Metabolic pathway regulation
  • Metabolic pathway optimization using functional genomics
  • Synthetic biology
  • Development of biosensors

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Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum

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Title
Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum
Author
Kim, SangwooJang, Yu-SinHa, Sung-ChulAhn, Jae-WooKim, Eun-JungLim, Jae HongCho, ChangheeRyu, Yong ShinLee, Sung KukLee, Sang YupKim, Kyung-Jin
Issue Date
2015-09
Publisher
NATURE PUBLISHING GROUP
Citation
NATURE COMMUNICATIONS, v.6, pp.8410
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/18061
URL
http://www.nature.com/ncomms/2015/150922/ncomms9410/full/ncomms9410.html
DOI
10.1038/ncomms9410
ISSN
2041-1723
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ECHE_Journal Papers
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