Structural insights of the MenD from Escherichia coli reveal ThDP affinity
DC Field | Value | Language |
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dc.contributor.author | Priyadarshi, Amit | - |
dc.contributor.author | Saleem, Yasar | - |
dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Kim, Key-Sun | - |
dc.contributor.author | Park, Sam-Yong | - |
dc.contributor.author | Kim, Eunice EunKyeong | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2021-09-08T18:51:05Z | - |
dc.date.available | 2021-09-08T18:51:05Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2009-03-20 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/120414 | - |
dc.description.abstract | MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration. (C) 2009 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | MENAQUINONE BIOSYNTHESIS | - |
dc.subject | (1R,6R)-2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE | - |
dc.subject | IDENTIFICATION | - |
dc.subject | DIPHOSPHATE | - |
dc.title | Structural insights of the MenD from Escherichia coli reveal ThDP affinity | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.01.168 | - |
dc.identifier.scopusid | 2-s2.0-60849134816 | - |
dc.identifier.wosid | 000264271100015 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.380, no.4, pp.797 - 801 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 380 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 797 | - |
dc.citation.endPage | 801 | - |
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.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | MENAQUINONE BIOSYNTHESIS | - |
dc.subject.keywordPlus | (1R,6R)-2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | DIPHOSPHATE | - |
dc.subject.keywordAuthor | Menaquinone | - |
dc.subject.keywordAuthor | MenD | - |
dc.subject.keywordAuthor | ThDP | - |
dc.subject.keywordAuthor | Oxoglutarate | - |
dc.subject.keywordAuthor | Decarboxylase | - |
dc.subject.keywordAuthor | Transferase | - |
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