DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Juhan | ko |
dc.contributor.author | Kyung, Dohyun | ko |
dc.contributor.author | Yun, Hyungdon | ko |
dc.contributor.author | Cho, Byung-Kwan | ko |
dc.contributor.author | Seo, Joo-Hyun | ko |
dc.contributor.author | Cha, Minho | ko |
dc.contributor.author | Kim, Byung-Gee | ko |
dc.date.accessioned | 2013-03-07T14:23:01Z | - |
dc.date.available | 2013-03-07T14:23:01Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2007-03 | - |
dc.identifier.citation | APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.73, no.6, pp.1772 - 1782 | - |
dc.identifier.issn | 0099-2240 | - |
dc.identifier.uri | http://hdl.handle.net/10203/90393 | - |
dc.description.abstract | A novel beta-transaminase gene was cloned from Mesorhizobium sp. strain LUK. By using N-terminal sequence and an internal protein sequence, a digoxigenin-labeled probe was made for nonradioactive hybridization, and a 2.5-kb gene fragment was obtained by colony hybridization of a cosmid library. Through Southern blotting and sequence analysis of the selected cosmid clone, the structural gene of the enzyme (1,335 bp) was identified, which encodes a protein of 47,244 Da with a theoretical pI of 6.2. The deduced amino acid sequence of the P-transaminase showed the highest sequence similarity with glutamate-l-semialdehyde aminomutase of transaminase subgroup II. The beta-transaminase showed higher activities toward D-beta-aminocarboxylic acids such as 3-aminobutyric acid, 3-amino-5-methylhexanoic acid, and 3-amino-3-phenylpropionic acid. The beta-transaminase has an unusually broad specificity for amino acceptors such as pyruvate and alpha-ketoglutarate/ oxaloacetate. The enantioselectivity of the enzyme suggested that the recognition mode of beta-aminocarboxylic acids in the active site is reversed relative to that of alpha-amino acids. After comparison of its primary structure with transaminase subgroup II enzymes, it was proposed that R43 interacts with the carboxylate group of the beta-aminocarboxylic acids and the carboxylate group on the side chain of dicarboxylic alpha-keto acids such as alpha-ketoglutarate and oxaloacetate. R404 is another conserved residue, which interacts with the alpha-carboxylate group of the ot-amino acids and alpha-keto acids. The P-transaminase was used for the asymmetric synthesis of enantiomerically pure beta-aminocarboxylic acids. (3S)-Amino-3-phenylpropionic acid was produced from the ketocarboxylic acid ester substrate by coupled reaction with a lipase using 3-aminobutyric acid as amino donor. | - |
dc.language | English | - |
dc.publisher | Amer Soc Microbiology | - |
dc.subject | LARGE-SCALE SYNTHESIS | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | ASPARTATE-AMINOTRANSFERASE | - |
dc.subject | ASYMMETRIC-SYNTHESIS | - |
dc.subject | SUBSTRATE RECOGNITION | - |
dc.subject | PYRUVATE TRANSAMINASE | - |
dc.subject | L-HOMOPHENYLALANINE | - |
dc.subject | CRYSTAL-STRUCTURES | - |
dc.subject | PURIFICATION | - |
dc.subject | RESOLUTION | - |
dc.title | Cloning and characterization of a novel beta-transaminase from Mesorhizobium sp Strain LUK: a new biocatalyst for the synthesis of enantiomerically pure beta-amino acids | - |
dc.type | Article | - |
dc.identifier.wosid | 000245156800011 | - |
dc.identifier.scopusid | 2-s2.0-33947373960 | - |
dc.type.rims | ART | - |
dc.citation.volume | 73 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 1772 | - |
dc.citation.endingpage | 1782 | - |
dc.citation.publicationname | APPLIED AND ENVIRONMENTAL MICROBIOLOGY | - |
dc.identifier.doi | 10.1128/AEM.02119-06 | - |
dc.contributor.localauthor | Cho, Byung-Kwan | - |
dc.contributor.nonIdAuthor | Kim, Juhan | - |
dc.contributor.nonIdAuthor | Kyung, Dohyun | - |
dc.contributor.nonIdAuthor | Yun, Hyungdon | - |
dc.contributor.nonIdAuthor | Seo, Joo-Hyun | - |
dc.contributor.nonIdAuthor | Cha, Minho | - |
dc.contributor.nonIdAuthor | Kim, Byung-Gee | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | LARGE-SCALE SYNTHESIS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ASPARTATE-AMINOTRANSFERASE | - |
dc.subject.keywordPlus | ASYMMETRIC-SYNTHESIS | - |
dc.subject.keywordPlus | SUBSTRATE RECOGNITION | - |
dc.subject.keywordPlus | PYRUVATE TRANSAMINASE | - |
dc.subject.keywordPlus | L-HOMOPHENYLALANINE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | RESOLUTION | - |
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