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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 638 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 631 | - |
dc.citation.title | NATURE CHEMICAL BIOLOGY | - |
dc.citation.volume | 7 | - |
dc.contributor.author | Lee, Seung Seo | - |
dc.contributor.author | Hong, Sung You | - |
dc.contributor.author | Errey, James C. | - |
dc.contributor.author | Izumi, Atsushi | - |
dc.contributor.author | Davies, Gideon J. | - |
dc.contributor.author | Davis, Benjamin G. | - |
dc.date.accessioned | 2023-12-22T05:47:11Z | - |
dc.date.available | 2023-12-22T05:47:11Z | - |
dc.date.created | 2013-07-31 | - |
dc.date.issued | 2011-09 | - |
dc.description.abstract | A previously determined crystal structure of the ternary complex of trehalose-6-phosphate synthase identified a putative transition state-like arrangement based on validoxylamine A 6'-O-phosphate and uridine diphosphate in the active site. Here linear free energy relationships confirm that these inhibitors are synergistic transition state mimics, supporting front-face nucleophilic attack involving hydrogen bonding between leaving group and nucleophile. Kinetic isotope effects indicate a highly dissociative oxocarbenium ion-like transition state. Leaving group O-18 effects identified isotopically sensitive bond cleavages and support the existence of a hydrogen bond between the nucleophile and departing group. Bronsted analysis of nucleophiles and Taft analysis highlight participation of the nucleophile in the transition state, also consistent with a front-face mechanism. Together, these comprehensive, quantitative data substantiate this unusual enzymatic reaction mechanism. Its discovery should prompt useful reassessment of many biocatalysts and their substrates and inhibitors. | - |
dc.identifier.bibliographicCitation | NATURE CHEMICAL BIOLOGY, v.7, no.9, pp.631 - 638 | - |
dc.identifier.doi | 10.1038/NCHEMBIO.628 | - |
dc.identifier.issn | 1552-4450 | - |
dc.identifier.scopusid | 2-s2.0-84860389788 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/3821 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84860389788 | - |
dc.identifier.wosid | 000294381400014 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Mechanistic evidence for a front-side, S(N)i-type reaction in a retaining glycosyltransferase | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | SUBSTRATE-ASSISTED CATALYSIS | - |
dc.subject.keywordPlus | ENZYMATIC GLYCOSYL TRANSFER | - |
dc.subject.keywordPlus | TRANSITION-STATE | - |
dc.subject.keywordPlus | ALPHA-GALACTOSYLTRANSFERASE | - |
dc.subject.keywordPlus | TREHALOSE PHOSPHORYLASE | - |
dc.subject.keywordPlus | NEISSERIA-MENINGITIDIS | - |
dc.subject.keywordPlus | SCHIZOPHYLLUM-COMMUNE | - |
dc.subject.keywordPlus | COVALENT INTERMEDIATE | - |
dc.subject.keywordPlus | GLUCOSYL TRANSFER | - |
dc.subject.keywordPlus | ACTIVE-SITE | - |
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