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Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.


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.

SUBMITTER: Kim S 

PROVIDER: S-EPMC4595758 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.

Kim Sangwoo S   Jang Yu-Sin YS   Ha Sung-Chul SC   Ahn Jae-Woo JW   Kim Eun-Jung EJ   Lim Jae Hong JH   Cho Changhee C   Ryu Yong Shin YS   Lee Sung Kuk SK   Lee Sang Yup SY   Kim Kyung-Jin KJ  

Nature communications 20150922


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 disu  ...[more]

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