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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/21671
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dc.contributor.authorKhandekar, S. S.en
dc.contributor.authorKonstantinidis, A. K.en
dc.contributor.authorSilverman, C.en
dc.contributor.authorJanson, C. A.en
dc.contributor.authorMcNulty, D. E.en
dc.contributor.authorNwagwu, S.en
dc.contributor.authorVan Aller, G. S.en
dc.contributor.authorDoyle, M. L.en
dc.contributor.authorKane, J. F.en
dc.contributor.authorQiu, X.en
dc.contributor.authorLonsdale, J.en
dc.date.accessioned2015-11-24T19:16:30Z-
dc.date.available2015-11-24T19:16:30Z-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21671-
dc.rightsDefault Licence-
dc.subject3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/biosynthesis/*chemistry/geneticsen
dc.subjectAcetyl Coenzyme A/*chemistryen
dc.subjectChromatography, Gelen
dc.subjectCircular Dichroismen
dc.subjectCrystallizationen
dc.subjectEscherichia coli/*enzymology/geneticsen
dc.subjectMass Spectrometryen
dc.subjectRecombinant Proteins/biosynthesis/chemistryen
dc.subjectSelenomethionine/*chemistry/metabolismen
dc.titleExpression, purification, and crystallization of the Escherichia coli selenomethionyl beta-ketoacyl-acyl carrier protein synthase IIIen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1006/bbrc.2000.2380-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/10733911-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0006291X00923805/1-s2.0-S0006291X00923805-main.pdf?_tid=9b16a2a26c4539e4d05e573809b27fd0&acdnat=1333958756_b47dae7b9cabaa501f89980701018889-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2000-
heal.abstractBacterial beta-ketoacyl-acyl carrier protein (ACP) synthase III (KAS III, also called FabH) catalyzes the condensation and transacylation of acetyl-CoA with malonyl-ACP. In order to understand the mode of enzyme/substrate interaction and design small molecule inhibitors, we have expressed, purified, and crystallized a selenomethionyl-derivative of E. coli KAS III. Several lines of evidence confirmed that purified selenomethionyl KAS III was homogenous, stably folded, and enzymatically active. Dynamic light scattering, size exclusion chromatography, and mass spectrometry results indicated that selenomethionyl KAS III is a noncovalent homodimer. Diffraction quality crystals of selenomethionyl KAS III/acetyl-CoA complex, which grew overnight to a size of 0.2 mm(3), belonged to the tetragonal space group P4(1)2(1)2.en
heal.journalNameBiochem Biophys Res Communen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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