Full metadata record
DC Field | Value | Language |
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dc.citation.startPage | 8410 | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 6 | - |
dc.contributor.author | Kim, Sangwoo | - |
dc.contributor.author | Jang, Yu-Sin | - |
dc.contributor.author | Ha, Sung-Chul | - |
dc.contributor.author | Ahn, Jae-Woo | - |
dc.contributor.author | Kim, Eun-Jung | - |
dc.contributor.author | Lim, Jae Hong | - |
dc.contributor.author | Cho, Changhee | - |
dc.contributor.author | Ryu, Yong Shin | - |
dc.contributor.author | Lee, Sung Kuk | - |
dc.contributor.author | Lee, Sang Yup | - |
dc.contributor.author | Kim, Kyung-Jin | - |
dc.date.accessioned | 2023-12-22T00:43:37Z | - |
dc.date.available | 2023-12-22T00:43:37Z | - |
dc.date.created | 2016-01-06 | - |
dc.date.issued | 2015-09 | - |
dc.description.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. | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.6, pp.8410 | - |
dc.identifier.doi | 10.1038/ncomms9410 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.scopusid | 2-s2.0-84942162949 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/18061 | - |
dc.identifier.url | http://www.nature.com/ncomms/2015/150922/ncomms9410/full/ncomms9410.html | - |
dc.identifier.wosid | 000363138400002 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | PEROXISOMAL 3-KETOACYL-COA THIOLASE | - |
dc.subject.keywordPlus | FERMENTATIVE BUTANOL PRODUCTION | - |
dc.subject.keywordPlus | ALLOSTERIC DISULFIDE BONDS | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | BIOSYNTHETIC THIOLASE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | SUBSTRATE-BINDING | - |
dc.subject.keywordPlus | DEPENDENT ENZYME | - |
dc.subject.keywordPlus | SOLVENTOGENESIS | - |
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