DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, SJ | ko |
dc.contributor.author | Kang, HY | ko |
dc.contributor.author | Lee, Younghoon | ko |
dc.date.accessioned | 2009-09-29T07:52:40Z | - |
dc.date.available | 2009-09-29T07:52:40Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-12 | - |
dc.identifier.citation | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.26, no.3-6, pp.265 - 272 | - |
dc.identifier.issn | 1381-1177 | - |
dc.identifier.uri | http://hdl.handle.net/10203/11592 | - |
dc.description.abstract | More and more, aldolases are being recognized as useful catalysts that carry out the reversible addition of a ketone donor to an aldehyde acceptor in achieving high stereoselectivity. Threonine aldolases catalyze the synthesis of variable P-hydroxy-alpha-amino acids, which are important structural units of various antibiotics and inummosuppressants. However, the enzymatic properties need to be improved to support a broader application to synthetic chemistry. Although directed-evolution is a powerful tool for improving enzymatic properties, the successful outcome depends on the efficiency of screening systems. We designed and proposed two high-throughput screening schemes for selecting L-threonine aldolase mutants with improved properties. These schemes utilized the toxicity of aldehyde, which acts as an acceptor in the aldol condensation. In these schemes, the following occurs: (1) the higher L-threonine aldolase activity reduces the toxic effect of aldehyde, which leads to the survival of the corresponding clone (the positive-selection scheme), and (2) the higher L-threonine aldolase activity produces more toxic aldehyde, which causes the death of the corresponding clone (the negative-selection scheme). According to the positive-selection scheme, we successfully selected L-threonine aldolase mutants with higher activities than the wild-type, from a randomly generated LTA library. (C) 2003 Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | ALPHA-AMINO ACIDS | - |
dc.subject | DIRECTED EVOLUTION | - |
dc.subject | ORGANIC-SYNTHESIS | - |
dc.subject | CHEMOENZYMATIC SYNTHESIS | - |
dc.subject | CATALYZED REACTION | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | KEY INTERMEDIATE | - |
dc.subject | GENE CLONING | - |
dc.subject | ENZYMES | - |
dc.subject | BIOCATALYSIS | - |
dc.title | High-throughput screening methods for selecting L-threonine aldolases with improved activity | - |
dc.type | Article | - |
dc.identifier.wosid | 000187060500020 | - |
dc.identifier.scopusid | 2-s2.0-0242659239 | - |
dc.type.rims | ART | - |
dc.citation.volume | 26 | - |
dc.citation.issue | 3-6 | - |
dc.citation.beginningpage | 265 | - |
dc.citation.endingpage | 272 | - |
dc.citation.publicationname | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, Younghoon | - |
dc.contributor.nonIdAuthor | Lee, SJ | - |
dc.contributor.nonIdAuthor | Kang, HY | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | aldehyde | - |
dc.subject.keywordAuthor | L-threonine aldolase | - |
dc.subject.keywordAuthor | directed-evolution | - |
dc.subject.keywordAuthor | high-throughput screening | - |
dc.subject.keywordAuthor | Pseudomonas aeruginosa | - |
dc.subject.keywordPlus | ALPHA-AMINO ACIDS | - |
dc.subject.keywordPlus | DIRECTED EVOLUTION | - |
dc.subject.keywordPlus | ORGANIC-SYNTHESIS | - |
dc.subject.keywordPlus | CHEMOENZYMATIC SYNTHESIS | - |
dc.subject.keywordPlus | CATALYZED REACTION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | KEY INTERMEDIATE | - |
dc.subject.keywordPlus | GENE CLONING | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordPlus | BIOCATALYSIS | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.