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Article: Suicide inhibition of α-oxamine synthases: Structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine

TitleSuicide inhibition of α-oxamine synthases: Structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine
Authors
Issue Date2006
PublisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/obc
Citation
Organic And Biomolecular Chemistry, 2006, v. 4 n. 7, p. 1209-1212 How to Cite?
AbstractThe suicide inhibition of the α-oxamine synthases by the substrate analog, L-trifluoroalanine was investigated. The inhibition resulted in the formation of a complex with loss of all three fluorine atoms. Decarboxylation and loss of fluoride occurred immediately after aldimine formation. The inherent flexibility could allow the difluorinated intermediate complex to adopt a suitable conformation. Decarboxylation in the normal mechanism occurs after formation of the ketoacid intermediate.
Persistent Identifierhttp://hdl.handle.net/10722/154394
ISSN
2015 Impact Factor: 3.559
2015 SCImago Journal Rankings: 1.464
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorAlexeev, Den_US
dc.contributor.authorBaxter, RLen_US
dc.contributor.authorCampopiano, DJen_US
dc.contributor.authorKerbarh, Oen_US
dc.contributor.authorSawyer, Len_US
dc.contributor.authorTomczyk, Nen_US
dc.contributor.authorWatt, Ren_US
dc.contributor.authorWebster, SPen_US
dc.date.accessioned2012-08-08T08:25:04Z-
dc.date.available2012-08-08T08:25:04Z-
dc.date.issued2006en_US
dc.identifier.citationOrganic And Biomolecular Chemistry, 2006, v. 4 n. 7, p. 1209-1212en_US
dc.identifier.issn1477-0520en_US
dc.identifier.urihttp://hdl.handle.net/10722/154394-
dc.description.abstractThe suicide inhibition of the α-oxamine synthases by the substrate analog, L-trifluoroalanine was investigated. The inhibition resulted in the formation of a complex with loss of all three fluorine atoms. Decarboxylation and loss of fluoride occurred immediately after aldimine formation. The inherent flexibility could allow the difluorinated intermediate complex to adopt a suitable conformation. Decarboxylation in the normal mechanism occurs after formation of the ketoacid intermediate.en_US
dc.languageengen_US
dc.publisherRoyal Society of Chemistry. The Journal's web site is located at http://www.rsc.org/obcen_US
dc.relation.ispartofOrganic and Biomolecular Chemistryen_US
dc.subject.meshAcyltransferases - Antagonists & Inhibitors - Chemistry - Metabolismen_US
dc.subject.meshAlanine - Analogs & Derivatives - Metabolismen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCatalysisen_US
dc.subject.meshHydrolysisen_US
dc.subject.meshLigases - Antagonists & Inhibitorsen_US
dc.subject.meshLysine - Chemistryen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshProtein Conformationen_US
dc.titleSuicide inhibition of α-oxamine synthases: Structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanineen_US
dc.typeArticleen_US
dc.identifier.emailWatt, R:rmwatt@hku.hken_US
dc.identifier.authorityWatt, R=rp00043en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1039/b517922jen_US
dc.identifier.pmid16557306-
dc.identifier.scopuseid_2-s2.0-33645306330en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33645306330&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume4en_US
dc.identifier.issue7en_US
dc.identifier.spage1209en_US
dc.identifier.epage1212en_US
dc.identifier.isiWOS:000236236900004-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridAlexeev, D=6701529096en_US
dc.identifier.scopusauthoridBaxter, RL=26643014900en_US
dc.identifier.scopusauthoridCampopiano, DJ=6602680734en_US
dc.identifier.scopusauthoridKerbarh, O=24576857900en_US
dc.identifier.scopusauthoridSawyer, L=7102690704en_US
dc.identifier.scopusauthoridTomczyk, N=12795469300en_US
dc.identifier.scopusauthoridWatt, R=7102907536en_US
dc.identifier.scopusauthoridWebster, SP=7101874218en_US

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