File Download

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher

박성훈

Park, Sunghoon
Biochemical Engineering Lab.
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Full metadata record

DC Field Value Language
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 -

qrcode

Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.