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dc.contributor.authorWu, Linrui
dc.contributor.authorTong, Ming Him
dc.contributor.authorRaab, Andrea
dc.contributor.authorFang, Qing
dc.contributor.authorWang, Shan
dc.contributor.authorKyeremeh, Kwaku
dc.contributor.authorYu, Yi
dc.contributor.authorDeng, Hai
dc.date.accessioned2020-04-23T12:30:02Z
dc.date.available2020-04-23T12:30:02Z
dc.date.issued2020-05
dc.identifier.citationWu , L , Tong , M H , Raab , A , Fang , Q , Wang , S , Kyeremeh , K , Yu , Y & Deng , H 2020 , ' An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions ' , Applied Microbiology and Biotechnology , vol. 104 , pp. 3885-3896 . https://doi.org/10.1007/s00253-020-10497-zen
dc.identifier.issn0175-7598
dc.identifier.otherPURE: 157854849
dc.identifier.otherPURE UUID: 1c2f784f-7aba-4f6a-970a-6fc2355a9de9
dc.identifier.otherWOS: 000518304700001
dc.identifier.otherScopus: 85081635980
dc.identifier.otherPubMed: 32140842
dc.identifier.otherORCID: /0000-0003-2058-0105/work/72630959
dc.identifier.otherORCID: /0000-0002-8479-5482/work/75817054
dc.identifier.urihttps://hdl.handle.net/2164/14145
dc.descriptionOpen Access via the Springer Compact Agreement. This study was funded by IBioIC PhD studentship (LW), Leverhulme Trust Research Project (HD and MHT, project No. RPG-2014-418), The Elphinstone Scholarship of University of Aberdeen (QF), Leverhulme Trust-Royal Society Africa award (KK and HD, AA090088) and the jointly funded UK Medical Research Council – UK Department for International Development (MRC/DFID) Concordat agreement African Research Leaders Award (KK and HD, MR/S00520X/1), Biotechnology and Biological Sciences Research Council UK (HD and SW, BB/P00380X/1) and National Natural Science Foundation of China (31,570,033, 31,811,530,299, and 31,870,035 to YY), and the Royal Society-NSFC Newton Mobility Grant Award (IEC\NSFC\170,617 to HD and YY).en
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofApplied Microbiology and Biotechnologyen
dc.rightsOpen Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.en
dc.subjectbeta-Hydroxy-alpha-amino acidsen
dc.subject4-fluorothreonineen
dc.subject4-fluorothreonine transaldolaseen
dc.subjectTransaldolationen
dc.subjectStreptomyces spen
dc.subjectMA37en
dc.subjectALPHA-AMINO ACIDSen
dc.subjectFLUOROMETABOLITE BIOSYNTHESISen
dc.subjectFLUORINASE ENZYMEen
dc.subjectIDENTIFICATIONen
dc.subjectTHREONINEen
dc.subjectDISCOVERYen
dc.subjectCATTLEYAen
dc.subjectPRODUCERen
dc.subjectREVEALSen
dc.subjectPEPTIDEen
dc.subjectβ-Hydroxy-α-amino acidsen
dc.subjectStreptomyces sp. MA37en
dc.subjectQD Chemistryen
dc.subjectApplied Microbiology and Biotechnologyen
dc.subjectBiotechnologyen
dc.subjectMedical Research Council (MRC)en
dc.subjectMR/S00520X/1en
dc.subjectBiotechnology and Biological Sciences Research Council (BBSRC)en
dc.subjectBB/P00380X/1en
dc.subject.lccQDen
dc.titleAn unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactionsen
dc.typeJournal articleen
dc.contributor.institutionUniversity of Aberdeen.Chemistryen
dc.contributor.institutionUniversity of Aberdeen.Natural & Computing Sciencesen
dc.contributor.institutionUniversity of Aberdeen.Chemistry (Research Theme)en
dc.description.statusPeer revieweden
dc.description.versionPublisher PDFen
dc.identifier.doihttps://doi.org/10.1007/s00253-020-10497-z
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=85081635980&partnerID=8YFLogxKen


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