Pseudomonas aeruginosa 4-Amino-4-Deoxychorismate Lyase Spatial Conservation of an Active Site Tyrosine and Classification of Two Types of Enzyme 英文参考文献.docVIP

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Pseudomonas aeruginosa 4-Amino-4-Deoxychorismate Lyase Spatial Conservation of an Active Site Tyrosine and Classification of Two Types of Enzyme 英文参考文献.doc

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Pseudomonas aeruginosa 4-Amino-4-Deoxychorismate Lyase Spatial Conservation of an Active Site Tyrosine and Classification of Two Types of Enzyme 英文参考文献

Pseudomonasaeruginosa4-Amino-4-Deoxychorismate Lyase:SpatialConservationofanActiveSiteTyrosine andClassificationofTwoTypesofEnzyme PatrickE.F.O’Rourke,ThomasC.Eadsforth,PaulK.Fyfe,SharonM.Shepherd,WilliamN.Hunter* DivisionofBiologicalChemistryandDrugDiscovery,CollegeofLifeSciences,UniversityofDundee,Dundee,UnitedKingdom Abstract 4-Amino-4-deoxychorismate lyase (PabC) catalyzes the formation of 4-aminobenzoate, and release of pyruvate, during folatebiosynthesis.ThisisanessentialactivityforthegrowthofGram-negativebacteria,includingimportantpathogens such as Pseudomonas aeruginosa. A high-resolution (1.75A)? crystal structure of PabC from P. aeruginosa has been determined,andsequence-structurecomparisonswithorthologousstructuresarereported.Residuesaroundthepyridoxal 59-phosphatecofactorarehighlyconservedaddingsupporttoaspectsofamechanismgenericforenzymescarryingthat cofactor.However,wesuggestthatPabCcanbeclassifiedintotwogroupsdependinguponwhetheranactivesiteand structurallyconservedtyrosineisprovidedfromthepolypeptidethatmainlyformsanactivesiteorfromthepartnersubunit in the dimeric assembly. We considered that the conserved tyrosine might indicate a direct role in catalysis: that of providing a proton to reduce the olefin moiety of substrate as pyruvate is released. A threonine had previously been suggested to fulfill such a role prior to our observation of the structurally conserved tyrosine. We have been unable to elucidateanexperimentallydeterminedstructureofPabCincomplexwithligandstoinformonmechanismandsubstrate specificity.Thereforeweconstructedacomputationalmodelofthecatalyticintermediatedockedintotheenzymeactive site.Themodelsuggeststhattheconservedtyrosinehelpstocreateahydrophobicwallononesideoftheactivesitethat providesimportantinteractionstobindthecatalyticintermediate.However,thisresiduedoesnotappeartoparticipatein interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. The model and our comparisonsrathersupportthehyp