DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Jieun | ko |
dc.contributor.author | Kim, Yeo-Jin | ko |
dc.contributor.author | Choi, So Young | ko |
dc.contributor.author | Lee, Sang Yup | ko |
dc.contributor.author | Kim, Kyung-Jin | ko |
dc.date.accessioned | 2019-03-08T15:34:51Z | - |
dc.date.available | 2019-03-08T15:34:51Z | - |
dc.date.created | 2017-04-04 | - |
dc.date.created | 2017-04-04 | - |
dc.date.created | 2017-04-04 | - |
dc.date.issued | 2017-01 | - |
dc.identifier.citation | BIOTECHNOLOGY JOURNAL, v.12, no.1 | - |
dc.identifier.issn | 1860-6768 | - |
dc.identifier.uri | http://hdl.handle.net/10203/251121 | - |
dc.description.abstract | Polyhydroxyalkanoates (PHAs) are natural polyesters synthesized by numerous microorganisms as energy and reducing power storage materials, and have attracted much attention as substitutes for petroleum-based plastics. Here, we report the first crystal structure of Ralstonia eutropha PHA synthase (RePhaC1) at 1.8 angstrom resolution and structu-based mechanisms for PHA polymerization. RePhaC1 contains two distinct domains, the N-terminal (RePhaC1(ND)) and C-terminal (RePhaC1 (CD)) domains, and exists as a dimer. RePhaC1 (CD) catalyzes polymerization via non-processive ping-pong mechanism using a Cys-His-Asp catalytic triad. Molecular docking simulation of 3-hydroxybutyrylCoA to the active site of RePhaC1 (CD) reveals residues involved in the formation of 3-hydroxybutyrylCoA binding pocket and substrate binding tunnel. Comparative analysis with other polymerases elucidates how different classes of PHA synthases show different substrate specificities. Furthermore, we attempted structure-based protein engineering and developed a RePhaC1 mutant with enhanced PHA synthase activity. | - |
dc.language | English | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.title | Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms | - |
dc.type | Article | - |
dc.identifier.wosid | 000395638400016 | - |
dc.identifier.scopusid | 2-s2.0-85008881293 | - |
dc.type.rims | ART | - |
dc.citation.volume | 12 | - |
dc.citation.issue | 1 | - |
dc.citation.publicationname | BIOTECHNOLOGY JOURNAL | - |
dc.identifier.doi | 10.1002/biot.201600648 | - |
dc.contributor.localauthor | Lee, Sang Yup | - |
dc.contributor.nonIdAuthor | Kim, Jieun | - |
dc.contributor.nonIdAuthor | Kim, Yeo-Jin | - |
dc.contributor.nonIdAuthor | Kim, Kyung-Jin | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordAuthor | Enzyme mechanism | - |
dc.subject.keywordAuthor | PHA synthase | - |
dc.subject.keywordAuthor | Polyhydroxyalkanoates | - |
dc.subject.keywordAuthor | Ralstonia eutropha | - |
dc.subject.keywordPlus | POLY-BETA-HYDROXYBUTYRATE | - |
dc.subject.keywordPlus | POLYHYDROXYBUTYRATE SYNTHASE | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | PHA SYNTHASE | - |
dc.subject.keywordPlus | ALCALIGENES-EUTROPHUS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | IN-VIVO | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | BIOSYNTHESIS | - |
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