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Redirection of pyruvate flux toward desired metabolic pathways through substrate channeling between pyruvate kinase and pyruvate-converting enzymes in Saccharomyces cerevisiae
DC Field | Value | Language |
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dc.contributor.author | Kim, Sujin | - |
dc.contributor.author | Bae, Sang-Jeong | - |
dc.contributor.author | Hahn, Ji-Sook | - |
dc.date.accessioned | 2023-04-19T08:48:49Z | - |
dc.date.available | 2023-04-19T08:48:49Z | - |
dc.date.created | 2018-06-29 | - |
dc.date.issued | 2016-04 | - |
dc.identifier.citation | Scientific Reports, Vol.6, p. 24145 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | https://hdl.handle.net/10371/191188 | - |
dc.description.abstract | Spatial organization of metabolic enzymes allows substrate channeling, which accelerates processing of intermediates. Here, we investigated the effect of substrate channeling on the flux partitioning at a metabolic branch point, focusing on pyruvate metabolism in Saccharomyces cerevisiae. As a platform strain for the channeling of pyruvate flux, PYK1-Coh-Myc strain was constructed in which PYK1 gene encoding pyruvate kinase is tagged with cohesin domain. By using high-affinity cohesin-dockerin interaction, the pyruvate-forming enzyme Pyk1 was tethered to heterologous pyruvate-converting enzymes, lactate dehydrogenase and a-acetolactate synthase, to produce lactic acid and 2,3-butanediol, respectively. Pyruvate flux was successfully redirected toward desired pathways, with a concomitant decrease in ethanol production even without genetic attenuation of the ethanol-producing pathway. This pyruvate channeling strategy led to an improvement of 2,3-butanediol production by 38%, while showing a limitation in improving lactic acid production due to a reduced activity of lactate dehydrogenase by dockerin tagging. | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Redirection of pyruvate flux toward desired metabolic pathways through substrate channeling between pyruvate kinase and pyruvate-converting enzymes in Saccharomyces cerevisiae | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/srep24145 | - |
dc.citation.journaltitle | Scientific Reports | - |
dc.identifier.wosid | 000373573400002 | - |
dc.identifier.scopusid | 2-s2.0-84963655914 | - |
dc.citation.startpage | 24145 | - |
dc.citation.volume | 6 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Hahn, Ji-Sook | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | LACTATE-DEHYDROGENASE GENE | - |
dc.subject.keywordPlus | L-LACTIC ACID | - |
dc.subject.keywordPlus | EFFICIENT PRODUCTION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | 2,3-BUTANEDIOL | - |
dc.subject.keywordPlus | SCAFFOLD | - |
dc.subject.keywordPlus | BIOSYNTHESIS | - |
dc.subject.keywordPlus | ORGANIZATION | - |
dc.subject.keywordPlus | CHEMICALS | - |
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