There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 765 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 752 | - |
dc.citation.title | ENVIRONMENTAL MICROBIOLOGY | - |
dc.citation.volume | 22 | - |
dc.contributor.author | Son, Hyeoncheol Francis | - |
dc.contributor.author | Kim, Sangwoo | - |
dc.contributor.author | Seo, Hogyun | - |
dc.contributor.author | Hong, Jiyeon | - |
dc.contributor.author | Lee, Donghoon | - |
dc.contributor.author | Jin, Kyeong Sik | - |
dc.contributor.author | Park, Sunghoon | - |
dc.contributor.author | Kim, Kyung-Jin | - |
dc.date.accessioned | 2023-12-21T18:07:29Z | - |
dc.date.available | 2023-12-21T18:07:29Z | - |
dc.date.created | 2020-01-23 | - |
dc.date.issued | 2020-02 | - |
dc.description.abstract | The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme. | - |
dc.identifier.bibliographicCitation | ENVIRONMENTAL MICROBIOLOGY, v.22, no.2, pp.752 - 765 | - |
dc.identifier.doi | 10.1111/1462-2920.14885 | - |
dc.identifier.issn | 1462-2912 | - |
dc.identifier.scopusid | 2-s2.0-85076756241 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/49314 | - |
dc.identifier.url | https://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/1462-2920.14885 | - |
dc.identifier.wosid | 000503551700001 | - |
dc.language | 영어 | - |
dc.publisher | Blackwell Publishing Inc. | - |
dc.title | Structural insight into bi-functional malonyl-CoA reductase | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.type.docType | Article; Early Access | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | AUTOTROPHIC CARBON FIXATION | - |
dc.subject.keywordPlus | COENZYME-A REDUCTASE | - |
dc.subject.keywordPlus | 3-HYDROXYPROPIONATE CYCLE | - |
dc.subject.keywordPlus | CHLOROFLEXUS-AURANTIACUS | - |
dc.subject.keywordPlus | KEY ENZYME | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | ACID | - |
dc.subject.keywordPlus | REPLACEMENT | - |
dc.subject.keywordPlus | TOXICITY | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.