3,6-Anhydro-L-galactonate cycloisomerase from Vibrio sp strain EJY3: crystallization and X-ray crystallographic analysis
DC Field | Value | Language |
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dc.contributor.author | Lee, Saeyoung | - |
dc.contributor.author | Yun, Eun Ju | - |
dc.contributor.author | Kim, Kyoung Heon | - |
dc.contributor.author | Kim, Hye-Yeon | - |
dc.contributor.author | Choi, In-Geol | - |
dc.date.accessioned | 2021-09-03T02:19:32Z | - |
dc.date.available | 2021-09-03T02:19:32Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-09 | - |
dc.identifier.issn | 2053-230X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/82396 | - |
dc.description.abstract | 3,6-Anhydro-l-galactonate cycloisomerase (ACI), which is found in the marine bacterium Vibrio sp. strain EJY3, converts 3,6-anhydro-l-galactonate into 2-keto-3-deoxygalactonate. ACI is a key enzyme in the metabolic pathway of 3,6-anhydro-l-galactose (AHG). Study of AHG metabolism is important for the efficient fermentation of agar and biofuel production, because AHG is a sugar that is non-fermentable by commercial microorganisms. The aci gene from Vibrio sp. strain EJY3 was cloned, and the recombinant protein was overexpressed and crystallized in order to determine the structure and understand the function of the protein. The crystals diffracted to 2.2 angstrom resolution and belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 87.9, c = 143.5 angstrom. The Matthews coefficient was 2.3 angstrom 3 Da(-1), with a solvent content of 47%. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
dc.subject | ENOLASE SUPERFAMILY | - |
dc.subject | DIVERGENT EVOLUTION | - |
dc.subject | RED MACROALGAE | - |
dc.title | 3,6-Anhydro-L-galactonate cycloisomerase from Vibrio sp strain EJY3: crystallization and X-ray crystallographic analysis | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Kyoung Heon | - |
dc.contributor.affiliatedAuthor | Choi, In-Geol | - |
dc.identifier.doi | 10.1107/S2053230X17011797 | - |
dc.identifier.scopusid | 2-s2.0-85028826299 | - |
dc.identifier.wosid | 000409298600003 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.73, pp.511 - 514 | - |
dc.relation.isPartOf | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.volume | 73 | - |
dc.citation.startPage | 511 | - |
dc.citation.endPage | 514 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.subject.keywordPlus | ENOLASE SUPERFAMILY | - |
dc.subject.keywordPlus | DIVERGENT EVOLUTION | - |
dc.subject.keywordPlus | RED MACROALGAE | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactonate | - |
dc.subject.keywordAuthor | AHGA | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactonate cycloisomerase | - |
dc.subject.keywordAuthor | ACI | - |
dc.subject.keywordAuthor | AHG metabolism | - |
dc.subject.keywordAuthor | agarolytic pathway | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactose | - |
dc.subject.keywordAuthor | Vibrio | - |
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