A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii 英文参考文献.docVIP

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A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii 英文参考文献.doc

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A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii 英文参考文献

AUniqueDualActivityAminoAcidHydroxylasein Toxoplasmagondii ElizabethA.Gaskell1,JudithE.Smith1,JohnW.Pinney3,DaveR.Westhead2,GlennA.McConkey1* 1InstituteofIntegrativeandComparativeBiology,UniversityofLeeds,Leeds,UnitedKingdom,2InstituteofMolecularandCellularBiology,UniversityofLeeds,Leeds, UnitedKingdom,3FacultyofLifeSciences,UniversityofManchester,Manchester,UnitedKingdom Abstract ThegenomeoftheprotozoanparasiteToxoplasmagondiiwasfoundtocontaintwogenesencodingtyrosinehydroxylase; thatproduces L-DOPA.Theencodedenzymesmetabolizephenylalanineaswellastyrosinewithsubstratepreferencefor tyrosine.ThustheenzymescatabolizephenylalaninetotyrosineandtyrosinetoL-DOPA.Thecatalyticdomaindescriptiveof thisclassofenzymesisconserved withtheparasiteenzymeandexhibitssimilarkineticpropertiestometazoantyrosine hydroxylases, but contains a unique N-terminal extension with a signal sequence motif. One of the genes, TgAaaH1, is constitutivelyexpressedwhiletheothergene,TgAaaH2,isinducedduringformationofthebradyzoitesofthecyststagesof the life cycle. This is the first description of an aromatic amino acid hydroxylase in an apicomplexan parasite. Extensive searching of apicomplexan genome sequences revealed an ortholog in Neospora caninum but not in Eimeria, Cryptosporidium, Theileria, or Plasmodium. Possible role(s) of these bi-functional enzymes during host infection are discussed. Citation: Gaskell EA, Smith JE, Pinney JW, Westhead DR, McConkey GA (2009) A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii . PLoS ONE4(3):e4801.doi:10.1371/journal.pone.0004801 Editor:PauloLeeHo,InstitutoButantan,Brazil ReceivedSeptember3,2008;AcceptedDecember31,2008;PublishedMarch11,2009 Copyright: ? 2009 Gaskell 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: This work was supported by the British Bi