DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, SJ | ko |
dc.contributor.author | Lee, SangYup | ko |
dc.date.accessioned | 2011-01-28T01:38:59Z | - |
dc.date.available | 2011-01-28T01:38:59Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-09 | - |
dc.identifier.citation | JOURNAL OF BACTERIOLOGY, v.185, pp.5391 - 5397 | - |
dc.identifier.issn | 0021-9193 | - |
dc.identifier.uri | http://hdl.handle.net/10203/21887 | - |
dc.description.abstract | The biosynthetic pathway of medium-chain-length (MCL) polyhydroxyalkanoates (PHAs) from fatty acids has been established in fadB mutant Escherichia coli strain by expressing the MCL-PHA synthase gene. However, the enzymes that are responsible for the generation of (R)-3-hydroxyacyl coenzyme A (R3HA-CoAs), the substrates for PHA synthase, have not been thoroughly elucidated. Escherichia coli MaoC, which is homologous to Pseudomonas aeruginosa (R)-specific enoyl-CoA hydratase (PhaJ1), was identified and found to be important for PHA biosynthesis in a fadB mutant E. coli strain. When the MCL-PHA synthase gene was introduced, the fadB maoC double-mutant E. coli WB108, which is a derivative of E. coli W3110, accumulated 43% less amount of MCL-PHA from fatty acid compared with the fadB mutant E. coli WB101. The PHA biosynthetic capacity could be restored by plasmid-based expression of the maoC(Ec) gene in E. coli WB108. Also, E. coli W3110 possessing fully functional beta-oxidation pathway could produce MCL-PHA from fatty acid by the coexpression of the maoC(Ec) gene and the MCL-PHA synthase gene. For the enzymatic analysis, MaoC fused with His(6)-Tag at its C-terminal was expressed in E. coli and purified. Enzymatic analysis of tagged MaoC showed that MaoC has enoyl-CoA hydratase activity toward crotonyl-CoA. These results suggest that MaoC is a new enoyl-CoA hydratase involved in supplying (R)-3-hydroxyacyl-CoA from the beta-oxidation pathway to PHA biosynthetic pathway in the fadB mutant E. coli strain. | - |
dc.description.sponsorship | This work was supported by the National Research Laboratory Program (2000-N-NL-01-C-237) of the Ministry of Science and Technology, the Center for Ultramicrochemical Process Systems sponsored by KOSEF, and the BK21 project. Hardware support for computational analysis by the IBM-SUR program is greatly appreciated. We thank Y. Doi (RIKEN, Saitana, Japan) and Isabelle-S. Hinner (GBF, Braunschweig, Germany) for kindly providing us with plasmids pBSEB50 and pBBR1MCS, respectively. We also thank G. M. Church (Harvard Medical School) for the kind gift of plasmid pKO3. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.title | Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli | - |
dc.type | Article | - |
dc.identifier.wosid | 000185181500008 | - |
dc.identifier.scopusid | 2-s2.0-0042337274 | - |
dc.type.rims | ART | - |
dc.citation.volume | 185 | - |
dc.citation.beginningpage | 5391 | - |
dc.citation.endingpage | 5397 | - |
dc.citation.publicationname | JOURNAL OF BACTERIOLOGY | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, SangYup | - |
dc.contributor.nonIdAuthor | Park, SJ | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | ACID BETA-OXIDATION | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | AEROMONAS-CAVIAE | - |
dc.subject.keywordPlus | COA HYDRATASE | - |
dc.subject.keywordPlus | BACTERIAL POLYHYDROXYALKANOATES | - |
dc.subject.keywordPlus | MOLECULAR CHARACTERIZATION | - |
dc.subject.keywordPlus | HYDROXYBUTYRIC ACID | - |
dc.subject.keywordPlus | FATTY-ACIDS | - |
dc.subject.keywordPlus | PHAG GENE | - |
dc.subject.keywordPlus | CLONING | - |
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