DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Byung-Kwan | ko |
dc.contributor.author | Park, Hyung-Yeon | ko |
dc.contributor.author | Seo, Joo-Hyun | ko |
dc.contributor.author | Kinnera, Koteshwar | ko |
dc.contributor.author | Lee, Bon-Su | ko |
dc.contributor.author | Kim, Byung-Gee | ko |
dc.date.accessioned | 2013-03-04T15:37:41Z | - |
dc.date.available | 2013-03-04T15:37:41Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2004-11 | - |
dc.identifier.citation | BIOTECHNOLOGY AND BIOENGINEERING, v.88, no.4, pp.512 - 519 | - |
dc.identifier.issn | 0006-3592 | - |
dc.identifier.uri | http://hdl.handle.net/10203/83093 | - |
dc.description.abstract | An enzymatic resolution was carried out for the preparation of enriched beta-heterocyclic D-alanine derivatives using Escherichia coli aromatic L-amino acid transaminase. The excess of pyrazole, imidazole, or 1,2,4-triazole reacted with methyl-2-acetamidoacrylate in acetonitrile in the presence of potassium carbonate at 60degreesC, directly leading to make the potassium salt of the corresponding N-acetyl-beta-heterocyclic alanine derivatives. After the acidic deprotection of the N-acetyl group, 10 mM of racemic pyrazolylalanine, triazolylalanine, and imidazolylalanine were resolved to D-pyrazolylalanine, D-triazolylalanine, and D-imidazolylalanine with 46% (85% ee), 42% (72% ee), and 48% (95% ee) conversion yield in 18 h, respectively, using E. coli aromatic L-amino acid transaminase (EC 2.6.1.5). Although the three beta-heterocyclic L-alanine derivatives have similar molecular structures, they showed different reaction rates and enantioselectivities. The relative reactivities of the transaminase toward the beta-heterocyclic L-alanine derivatives could be explained by the relationship between the substrate binding energy (E, kcal/mol) to the enzyme active site and the distance (delta, Angstrom) from the nitrogen of a-amino group of the substrates to the C4' carbon of PLP-Lys258 Schiff base. As the ratio of the substrate binding energy (E) to the distance (delta) becomes indicative value of k(cat)/K-M of the enzyme to the substrate, the relative reactivities of the beta-heterocyclic L-alanine derivatives were successfully correlated with E/delta, and the relationship was confirmed by our experiments. (C) 2004 Wiley Periodicals, Inc. | - |
dc.language | English | - |
dc.publisher | JOHN WILEY & SONS INC | - |
dc.subject | INCREMENTAL CONSTRUCTION ALGORITHM | - |
dc.subject | PURE (S)-AMINO ACIDS | - |
dc.subject | ASPARTATE-AMINOTRANSFERASE | - |
dc.subject | CHEMOENZYMATIC SYNTHESIS | - |
dc.subject | SUBSTRATE-SPECIFICITY | - |
dc.subject | ASYMMETRIC-SYNTHESIS | - |
dc.subject | KINETIC RESOLUTION | - |
dc.subject | ACTIVE-SITE | - |
dc.subject | BINDING | - |
dc.subject | DOCKING | - |
dc.title | Enzymatic resolution for the preparation of enantiomerically enriched D-beta-heterocyclic alanine derivatives using Escherichia coli aromatic L-amino acid transaminase | - |
dc.type | Article | - |
dc.identifier.wosid | 000224852900010 | - |
dc.identifier.scopusid | 2-s2.0-8844239142 | - |
dc.type.rims | ART | - |
dc.citation.volume | 88 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 512 | - |
dc.citation.endingpage | 519 | - |
dc.citation.publicationname | BIOTECHNOLOGY AND BIOENGINEERING | - |
dc.identifier.doi | 10.1002/bit.20280 | - |
dc.contributor.localauthor | Cho, Byung-Kwan | - |
dc.contributor.nonIdAuthor | Park, Hyung-Yeon | - |
dc.contributor.nonIdAuthor | Seo, Joo-Hyun | - |
dc.contributor.nonIdAuthor | Kinnera, Koteshwar | - |
dc.contributor.nonIdAuthor | Lee, Bon-Su | - |
dc.contributor.nonIdAuthor | Kim, Byung-Gee | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | transaminase | - |
dc.subject.keywordAuthor | kinetic resolution | - |
dc.subject.keywordAuthor | beta-heterocyclic alanine derivatives | - |
dc.subject.keywordAuthor | reaction activity prediction | - |
dc.subject.keywordAuthor | substrate docking | - |
dc.subject.keywordPlus | INCREMENTAL CONSTRUCTION ALGORITHM | - |
dc.subject.keywordPlus | PURE (S)-AMINO ACIDS | - |
dc.subject.keywordPlus | ASPARTATE-AMINOTRANSFERASE | - |
dc.subject.keywordPlus | CHEMOENZYMATIC SYNTHESIS | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | ASYMMETRIC-SYNTHESIS | - |
dc.subject.keywordPlus | KINETIC RESOLUTION | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | DOCKING | - |
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