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• W2210361504 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." @default.
• W2210361504 created "2016-06-24" @default.
• W2210361504 creator A5008430104 @default.
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• W2210361504 date "2015-09-22" @default.
• W2210361504 modified "2023-10-10" @default.
• W2210361504 title "Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum" @default.
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• W2210361504 doi "https://doi.org/10.1038/ncomms9410" @default.
• W2210361504 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4595758" @default.
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• W2210361504 hasPublicationYear "2015" @default.
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