Remarkable Diversity in the Enzymes Catalyzing the Last Step in Synthesis of the Pimelate Moiety of Biotin 英文参考文献.docVIP

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Remarkable Diversity in the Enzymes Catalyzing the Last Step in Synthesis of the Pimelate Moiety of Biotin 英文参考文献.doc

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Remarkable Diversity in the Enzymes Catalyzing the Last Step in Synthesis of the Pimelate Moiety of Biotin 英文参考文献

RemarkableDiversityintheEnzymesCatalyzingtheLast StepinSynthesisofthePimelateMoietyofBiotin MadelynM.Shapiro1,VandanaChakravartty1,JohnE.Cronan1,2* 1DepartmentofMicrobiology,UniversityofIllinois,Urbana,Illinois,UnitedStatesofAmerica,2DepartmentofBiochemistry,UniversityofIllinois,Urbana,Illinois,United StatesofAmerica Abstract BiotinsynthesisinEscherichiacolirequiresthefunctionsofthebioHandbioCgenestosynthesizetheprecursorpimelate moietybyuseofamodifiedfattyacidbiosynthesispathway.However,itwaspreviouslynotedthatbioHhasbeenreplaced withbioGorbioKwithinthebiotinsyntheticgeneclustersofotherbacteria.WereportthateachoffourBioGproteinsfrom diverse bacteria and two cyanobacterial BioK proteins functionally replace E. coli BioH in vivo. Moreover, purified BioG proteins have esterase activity against pimeloyl-ACP methyl ester, the physiological substrate of BioH. Two of the BioG proteins block biotin synthesis when highly expressed and these toxic proteins were shown to have more promiscuous substratespecificitiesthanthenon-toxicBioGproteins.ApostulatedBioG-BioCfusionproteinwasshowntofunctionally replaceboththeBioHandBioCfunctionsofE.coli.AlthoughtheBioH,BioGandBioKesterasescatalyzeacommonreaction, theproteinsareevolutionarilydistinct. Citation:ShapiroMM,ChakravarttyV,CronanJE(2012)RemarkableDiversityintheEnzymesCatalyzingtheLastStepinSynthesisofthePimelateMoietyof Biotin.PLoSONE7(11):e49440.doi:10.1371/journal.pone.0049440 Editor:ChristopheHerman,BaylorCollegeofMedicine,UnitedStatesofAmerica ReceivedJuly23,2012;AcceptedOctober9,2012;PublishedNovember9,2012 Copyright: ? 2012 Shapiro et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding:FundingwasprovidedbyNIHNIAIDAI15650.Thefundershadnoroleinstudydesign,datacollectionandanalysis,decisiontopublish,orpreparation ofthemanuscript. CompetingInterest