Full metadata record
DC Field | Value | Language |
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dc.citation.startPage | 46005 | - |
dc.citation.title | SCIENTIFIC REPORTS | - |
dc.citation.volume | 7 | - |
dc.contributor.author | Son, Hyeoncheol Francis | - |
dc.contributor.author | Park, Sunghoon | - |
dc.contributor.author | Yoo, Tae Hyeon | - |
dc.contributor.author | Jung, Gyoo Yeol | - |
dc.contributor.author | Kim, Kyung-Jin | - |
dc.date.accessioned | 2023-12-21T22:20:12Z | - |
dc.date.available | 2023-12-21T22:20:12Z | - |
dc.date.created | 2017-05-08 | - |
dc.date.issued | 2017-04 | - |
dc.description.abstract | 3-Hydroxypropionic acid (3-HP) is an important platform chemical to be converted to acrylic acid and acrylamide. Aldehyde dehydrogenase (ALDH), an enzyme that catalyzes the reaction of 3-hydroxypropionaldehyde (3-HPA) to 3-HP, determines 3-HP production rate during the conversion of glycerol to 3-HP. To elucidate molecular mechanism of 3-HP production, we determined the first crystal structure of a 3-HP producing ALDH, alpha-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH), in its apo-form and in complex with NAD(+). Although showing an overall structure similar to other ALDHs, the AbKGSADH enzyme had an optimal substrate binding site for accepting 3-HPA as a substrate. Molecular docking simulation of 3-HPA into the AbKGSADH structure revealed that the residues Asn159, Gln160 and Arg163 stabilize the aldehyde-and the hydroxyl-groups of 3-HPA through hydrogen bonds, and several hydrophobic residues, such as Phe156, Val286, Ile288, and Phe450, provide the optimal size and shape for 3-HPA binding. We also compared AbKGSADH with other reported 3-HP producing ALDHs for the crucial amino acid residues for enzyme catalysis and substrate binding, which provides structural implications on how these enzymes utilize 3-HPA as a substrate. | - |
dc.identifier.bibliographicCitation | SCIENTIFIC REPORTS, v.7, pp.46005 | - |
dc.identifier.doi | 10.1038/srep46005 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.scopusid | 2-s2.0-85017345042 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/22234 | - |
dc.identifier.url | https://www.nature.com/articles/srep46005 | - |
dc.identifier.wosid | 000398965600001 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense | - |
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 | RECOMBINANT ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | AUTOTROPHIC CO2 FIXATION | - |
dc.subject.keywordPlus | KLEBSIELLA-PNEUMONIAE | - |
dc.subject.keywordPlus | UTILIZES 3-HYDROXYPROPIONALDEHYDE | - |
dc.subject.keywordPlus | GLYCEROL FERMENTATION | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | 1,3-PROPANEDIOL | - |
dc.subject.keywordPlus | SUBSTRATE | - |
dc.subject.keywordPlus | UPDATE | - |
dc.subject.keywordPlus | GENE | - |
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