DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Byung-Kwan | ko |
dc.contributor.author | Seo, Joo-Hyun | ko |
dc.contributor.author | Kang, Taek-Jin | ko |
dc.contributor.author | Kim, Juhan | ko |
dc.contributor.author | Park, Hyung-Yeon | ko |
dc.contributor.author | Lee, Bon-Su | ko |
dc.contributor.author | Kim, Byung-Gee | ko |
dc.date.accessioned | 2013-03-07T10:03:16Z | - |
dc.date.available | 2013-03-07T10:03:16Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006-08 | - |
dc.identifier.citation | BIOTECHNOLOGY AND BIOENGINEERING, v.94, no.5, pp.842 - 850 | - |
dc.identifier.issn | 0006-3592 | - |
dc.identifier.uri | http://hdl.handle.net/10203/89936 | - |
dc.description.abstract | An enzymatic asymmetric synthesis was carried out for the preparation of enantiomerically pure L-cliphenylalanine using the rationally engineered aromatic L-amino acid transaminase (eAroATEs) obtained from Enterobactersp. BK2K-1. To rationally redesign the enzyme, structural model was constructed by the homology modeling. The structural model was experimentally validated by the site-directed mutagenesis of the predicted pyridoxal-5'-phosphate (PLP) binding site and the substrate-recognition region, and the cell-free protein synthesis of mutated enzymes. It was suggested that Arg281 and Arg375 were the key residues to recognize the distal carboxylate and alpha-carboxylate group of the substrates, respectively. The model also predicted that Tyr66 forms hydrogen bond with the phosphate moiety of PLP and interacts with the side chain attached to beta-carbon of the amino acid substrate. Among the various site-directed mutants, Y66L variant was able to synthesize L-diphenylalanine with 23% conversion yield for 10 h, whereas the wild-type AroATEs was inactive for the transamination between cliphenylpyruvate and L-phenylalanine as amino acceptor and amino donor, respectively. (c) 2006 Wiley Periodicals, Inc. | - |
dc.language | English | - |
dc.publisher | JOHN WILEY & SONS INC | - |
dc.subject | FREE PROTEIN-SYNTHESIS | - |
dc.subject | ALPHA-METHYLBENZYLAMINE | - |
dc.subject | KINETIC RESOLUTION | - |
dc.subject | AMINOTRANSFERASE | - |
dc.subject | RECOGNITION | - |
dc.subject | DERIVATIVES | - |
dc.subject | SITE | - |
dc.subject | DEHYDROGENASES | - |
dc.subject | SYSTEM | - |
dc.subject | ESTERS | - |
dc.title | Engineering aromatic L-amino acid transaminase for the asymmetric synthesis of constrained analogs of L-phenylalanine | - |
dc.type | Article | - |
dc.identifier.wosid | 000239046900003 | - |
dc.identifier.scopusid | 2-s2.0-33746894637 | - |
dc.type.rims | ART | - |
dc.citation.volume | 94 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | 842 | - |
dc.citation.endingpage | 850 | - |
dc.citation.publicationname | BIOTECHNOLOGY AND BIOENGINEERING | - |
dc.identifier.doi | 10.1002/bit.20902 | - |
dc.contributor.localauthor | Cho, Byung-Kwan | - |
dc.contributor.nonIdAuthor | Seo, Joo-Hyun | - |
dc.contributor.nonIdAuthor | Kang, Taek-Jin | - |
dc.contributor.nonIdAuthor | Kim, Juhan | - |
dc.contributor.nonIdAuthor | Park, Hyung-Yeon | - |
dc.contributor.nonIdAuthor | Lee, Bon-Su | - |
dc.contributor.nonIdAuthor | Kim, Byung-Gee | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | FREE PROTEIN-SYNTHESIS | - |
dc.subject.keywordPlus | ALPHA-METHYLBENZYLAMINE | - |
dc.subject.keywordPlus | KINETIC RESOLUTION | - |
dc.subject.keywordPlus | AMINOTRANSFERASE | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | DERIVATIVES | - |
dc.subject.keywordPlus | SITE | - |
dc.subject.keywordPlus | DEHYDROGENASES | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | ESTERS | - |
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