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DC Field | Value | Language |
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dc.citation.endPage | 1024 | - |
dc.citation.startPage | 1015 | - |
dc.citation.title | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.citation.volume | 28 | - |
dc.contributor.author | Park, Ye Seop | - |
dc.contributor.author | Nasir, Abdul | - |
dc.contributor.author | Thuan Phu Nguyen-Vo | - |
dc.contributor.author | Ryu, Huichang | - |
dc.contributor.author | Seok, Joo Yeon | - |
dc.contributor.author | Jung, Gyoo Yeol | - |
dc.contributor.author | Park, Sunghoon | - |
dc.contributor.author | Yoo, Tae Hyeon | - |
dc.date.accessioned | 2023-12-21T14:07:20Z | - |
dc.date.available | 2023-12-21T14:07:20Z | - |
dc.date.created | 2023-11-09 | - |
dc.date.issued | 2023-12 | - |
dc.description.abstract | 3-Hydroxypropionic acid (3-HP) is a key building block for value-added chemicals. A biological route for synthesizing this molecule is two-step enzymatic reactions; dehydration of glycerol to 3-hydroxypropanal (3-HPA) by glycerol dehydratase and then oxidation of 3-HPA to 3-HP by aldehyde dehydrogenase. Here, we report an aldehyde dehydrogenase, an engineered alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH) from Azospirillum brasilense. The variant, named 2C10, was obtained by applying a large KGSADH library to a selection method based on a 3-HP-responsive transcription factor and then a screening method for observing the activities of individual clones. 2C10 exhibited a 4.65-fold higher catalytic activity (k(cat)/K-m: 100 +/- 7.1 s(-1)mM(-1)) toward 3-HPA than the wild-type enzyme. The flask culture of Pseudomonas denitrificans with 2C10 resulted in an approximately 30% increase in 3-HP titer (43.2 mM) compared with that obtained using wild-type KGSADH (33.1 mM). Molecular dynamics simulations suggested that compared to the wild-type enzyme, 2C10 has a less flexible and smaller binding pocket for aldehyde substrates. | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.28, pp.1015 - 1024 | - |
dc.identifier.doi | 10.1007/s12257-021-0335-3 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.scopusid | 2-s2.0-85132347444 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/66168 | - |
dc.identifier.wosid | 000814028500003 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
dc.title | Engineering of the Substrate Pocket of α-ketoglutaric Semialdehyde Dehydrogenase for Improving the Activity toward 3-hydroxypropanal | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.type.docType | Article; Early Access | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.subject.keywordAuthor | 3-Hydroxypropionic acid | - |
dc.subject.keywordAuthor | 3-Hydroxypropanal | - |
dc.subject.keywordAuthor | aldehyde dehydrogenase | - |
dc.subject.keywordAuthor | enzyme engineering | - |
dc.subject.keywordAuthor | molecular dynamics simulation | - |
dc.subject.keywordPlus | KLEBSIELLA-PNEUMONIAE | - |
dc.subject.keywordPlus | ALDEHYDE DEHYDROGENASE | - |
dc.subject.keywordPlus | UTILIZES 3-HYDROXYPROPIONALDEHYDE | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ACID PRODUCTION | - |
dc.subject.keywordPlus | GLYCEROL | - |
dc.subject.keywordPlus | DELETION | - |
dc.subject.keywordPlus | PATHWAY | - |
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