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DC Field | Value | Language |
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dc.citation.endPage | 60 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 51 | - |
dc.citation.title | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 81 | - |
dc.contributor.author | Jo, Ji-Eun | - |
dc.contributor.author | Raj, Subramanian Mohan | - |
dc.contributor.author | Rathnasingh, Chelladurai | - |
dc.contributor.author | Selvakumar, Edwardraja | - |
dc.contributor.author | Jung, Woo-Chel | - |
dc.contributor.author | Park, Sunghoon | - |
dc.date.accessioned | 2023-12-22T08:15:27Z | - |
dc.date.available | 2023-12-22T08:15:27Z | - |
dc.date.created | 2017-03-04 | - |
dc.date.issued | 2008-11 | - |
dc.description.abstract | 3-Hydroxypropionaldehyde (3-HPA), an intermediary compound of glycerol metabolism in bacteria, serves as a precursor to 3-Hydroxypropionic acid (3-HP), a commercially valuable platform chemical. To achieve the effective conversion of 3-HPA to 3-HP, an aldH gene encoding an aldehyde dehydrogenase in Escherichia coli K-12 (AldH) was cloned, expressed, and characterized for its properties. The recombinant AldH exhibited broad substrate specificity for various aliphatic and aromatic aldehydes. AldH preferred NAD(+) over NADP(+) as a cofactor for the oxidation of most aliphatic aldehydes tested. Among the aldehydes used, the specific activity was highest (38.1 U mg(-1) protein) for 3-HPA at pH 8.0 and 37 degrees C. The catalytic efficiency (k (cat)) and the specificity constant (k(cat)/K-m) for 3-HPA in the presence of NAD(+) were 28.5 s(-1) and 58.6 x 10(3) M-1 s(-1), respectively. The AldH activity was enhanced in the presence of disulfide reductants such as dithiothreitol (DTT) or 2-mercaptoethanol, while several metal ions, particularly Hg2+, Ag+, Cu2+, and Zn2+, inhibited AldH activity. This study illustrates that AldH is a potentially useful enzyme in converting 3-HPA to 3-HP. | - |
dc.identifier.bibliographicCitation | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.81, no.1, pp.51 - 60 | - |
dc.identifier.doi | 10.1007/s00253-008-1608-x | - |
dc.identifier.issn | 0175-7598 | - |
dc.identifier.scopusid | 2-s2.0-54349128839 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/25356 | - |
dc.identifier.url | https://link.springer.com/article/10.1007%2Fs00253-008-1608-x | - |
dc.identifier.wosid | 000260260600006 | - |
dc.language | 영어 | - |
dc.publisher | SPRINGER | - |
dc.title | Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-Hydroxypropionaldehyde as a substrate | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Aldehyde dehydrogenase | - |
dc.subject.keywordAuthor | aldH | - |
dc.subject.keywordAuthor | 3-Hydroxypropionaldehyde dehydrogenase | - |
dc.subject.keywordAuthor | 3-Hydroxypropionic acid | - |
dc.subject.keywordAuthor | Enzyme characterization | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | METABOLIC PATHWAYS | - |
dc.subject.keywordPlus | GENE-PRODUCT | - |
dc.subject.keywordPlus | ALD GENE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | EVOLUTION | - |
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