Methanol Assimilation in Methylobacterium extorquens AM1 Demonstration of All Enzymes and Their Regulation 英文参考文献.docVIP

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Methanol Assimilation in Methylobacterium extorquens AM1 Demonstration of All Enzymes and Their Regulation 英文参考文献.doc

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Methanol Assimilation in Methylobacterium extorquens AM1 Demonstration of All Enzymes and Their Regulation 英文参考文献

MethanolAssimilationinMethylobacteriumextorquens AM1:DemonstrationofAllEnzymesandTheir Regulation HanaSmejkalovaˇ ′,TobiasJ.Erb¤,GeorgFuchs* Mikrobiologie,Fakulta¨t fu¨rBiologie,Albert-Ludwigs-Universita¨t Freiburg,Freiburg,Germany Abstract Background: Methylobacterium extorquens AM1 is an aerobic facultative methylotrophic a-proteobacterium that can use reducedone-carboncompoundssuchasmethanol,butalsomulti-carbonsubstrateslikeacetate(C2)orsuccinate(C4 )as solecarbonandenergysource.Theorganismhasgainedinterestasfuturebiotechnologicalproductionplatformbasedon methanolasfeedstock. Methodology/Principal Findings: We present a comprehensive study of all postulated enzymes for the assimilation of methanolandtheirregulationinresponsetothecarbonsource.Formaldehyde,whichisderivedfrommethanoloxidation, is assimilated via the serine cycle, which starts with glyoxylate and forms acetyl-CoA. Acetyl-CoA is assimilated via the proposed ethylmalonyl-CoApathway, whichthereby regenerates glyoxylate. To furtherthe understandingof thecentral carbon metabolism we identified and quantified all enzymes of the pathways involved in methanol assimilation. We observedastrictdifferentialregulationoftheiractivityleveldependingonwhetherC1,C2orC4compoundsareused.The enzymes,whicharespecificallyrequiredfortheutilizationoftheindividualsubstrates,wereseveral-foldup-regulatedand thosenotrequiredweredown-regulated.Theenzymesoftheethylmalonyl-CoApathwayshowedspecificactivities,which werehigherthanthecalculatedminimalvaluesthatcanaccountfortheobservedgrowthrate.Yet,someenzymesofthe serinecycle,notablyitsfirstandlastenzymesserinehydroxymethyltransferaseandmalatethiokinase,exhibitmuchlower values and probably are rate limiting during methylotrophic growth. We identified the natural C1 carrying coenzyme as tetrahydropteroyl-tetraglutamateratherthantetrahydrofolate. Conclusion/Significance:Thisstudyprovidesthefirstcompletepictureoftheenzymesrequiredformethanolassimilation,the regulationoftheiract