Full metadata record
DC Field | Value | Language |
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dc.citation.startPage | 39587 | - |
dc.citation.title | SCIENTIFIC REPORTS | - |
dc.citation.volume | 6 | - |
dc.contributor.author | Lim, Sung In | - |
dc.contributor.author | Yang, Byungseop | - |
dc.contributor.author | Jung, Younghan | - |
dc.contributor.author | Cha, Jaehyun | - |
dc.contributor.author | Cho, Jinhwan | - |
dc.contributor.author | Choi, Eun-Sil | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.contributor.author | Kwon, Inchan | - |
dc.date.accessioned | 2023-12-21T22:50:28Z | - |
dc.date.available | 2023-12-21T22:50:28Z | - |
dc.date.created | 2016-12-23 | - |
dc.date.issued | 2016-12 | - |
dc.description.abstract | Multistep cascade reactions in nature maximize reaction efficiency by co-assembling related enzymes. Such organization facilitates the processing of intermediates by downstream enzymes. Previously, the studies on multienzyme nanocomplexes assembled on DNA scaffolds demonstrated that closer interenzyme distance enhances the overall reaction efficiency. However, it remains unknown how the active site orientation controlled at nanoscale can have an effect on multienzyme reaction. Here, we show that controlled alignment of active sites promotes the multienzyme reaction efficiency. By genetic incorporation of a non-natural amino acid and two compatible bioorthogonal chemistries, we conjugated mannitol dehydrogenase to formate dehydrogenase with the defined active site arrangement with the residue-level accuracy. The study revealed that the multienzyme complex with the active sites directed towards each other exhibits four-fold higher relative efficiency enhancement in the cascade reaction and produces 60% more D-mannitol than the other complex with active sites directed away from each other. | - |
dc.identifier.bibliographicCitation | SCIENTIFIC REPORTS, v.6, pp.39587 | - |
dc.identifier.doi | 10.1038/srep39587 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.scopusid | 2-s2.0-85006972570 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/21064 | - |
dc.identifier.url | http://www.nature.com/articles/srep39587 | - |
dc.identifier.wosid | 000390266800001 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex | - |
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 | NONCANONICAL AMINO-ACIDS | - |
dc.subject.keywordPlus | ENHANCED CATALYSIS | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | SCAFFOLDS | - |
dc.subject.keywordPlus | MANNITOL | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | FUSION | - |
dc.subject.keywordPlus | BIOCONJUGATION | - |
dc.subject.keywordPlus | IMMOBILIZATION | - |
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