锰过氧化物酶的结构与功能-胡明

*胡明卢雪梅**高培基(250100)综述了木素降解的关键酶之一锰过氧化物酶的三维分子结构和催化反应性能,综合概述了通过定点诱变等方法对锰过氧化物酶的结构和功能的研究进展锰过氧化物酶定点诱变黄孢原毛平革菌:2002-12-04*(29906005)(2000D11)**,:[e-mail]1,CO2H2O2080,Phanerochaetechrysosporium,(ligninperoxidase,LiP)(manganeseperoxidase,MnP),MnPMnÒ,MnP,,Phanerochaetechrysosporium,Dichomitussqualens,Ceriporiopsissubvermispora,Lentinusedodes,Trametesversicolor,Phlebiaradiata,PleurotuspstreatusPanustigrinus(Phanerochaetechrysosporium)LiP,LiP,,MnP2P.chrysosporiumMnP,pH412~415,45~47kDIX[1]H2O2(),MnPMnÒMnÓ,MnÓ,2,6-ABTS(2,2-azinobis)MnP11MnPAH:A#:[P+#]:P-MnPH2O2,ÑÑMnÒ,ÒMnÒ,ÒMnPH2O2MnPÓMnÒÑÒ,MnÒ233JOURNALOFCHINESEBIOTECHNOLOGY20033DOI10.13523/j.cb.20030307ÒMnP[2],,MnP[3]33.1MnPFeÓMnPHRP(horseradishperoxidase)LiP,[4]P.chrysosporium,MnPcDNA[5]MnP:3505,P.ChrysosporiumMnPMnPLiP,(MnP),,LiP,MnPLiP3.2MnP,FeÓ,P.chrysosporium,[1]MnP,,(2)[1]MnP,Asp47Ser66Asp64,Gly62Asp47,Glu74,Gln80His46BAsp47,2P.chrysosporiumMnPThr196Ser174Thr193,Asp191Thr193Asp198Ser174,Ser174His173[6]MnP,1-32-74-56-8,[7]MnP,,[1]313His46Ary42Asn80Glu74Phe45,His46,Arg42,,Ñ,Arg,MnP,Arg42Asn80Glu74His46,,His173Asp242Phe190His173,313:,,[1]3.4MnP,,,MnÒ,MnÓMnP,,[8]MnÒD-,NMR(nuclearmagneticresonance)11!MnPMnÒ,MnÒ[9]Mn(3),,(Glu35,Lu39Asp179)67,-21342182!Arg177Glu35,Glu35,Glu35,[1]MnÒ(0180!)MnÓ(0166!),MnÒMnÓ,MnÒMnÓ[9]3MnPMnE:Glu;D:Asp;R:Arg4-4.1P.chrysosporiumMnPEscherichiacoliAspergillusoryzaeE.coli,,E.colirMnP(recombinantMnP)wtMnP(wide-typeMnP)[10]rMnPA.cryzae,[11],,rMnPP.chrysosporium,wtMnP,wtMnP,P.chrysosporiummnp,,,,rMnP[12],Aspergillusniger,MnP[13]412X-(3)MnP,,Asp179AsnGlu35GlnGlu39GlnP.chrysosporiumMnPwtMnPwtMnP,,[14],,wtMnP,MnÒKm,kcatwtMnP,Mn,,Asp179Ala,Glu35AspGlu39Asp,Asp179AlaGlu35AspkcatKm,3223rMnP(kcatPKm)104[15],,Asp179,Glu35Glu39Arg177MnGlu35(3)Arg177(Arg177LysAry177Ala)MnÒKm,Mn,,MnÒ[16]MnPMnÒ:MnÒ,Arg177;MnÒ,Arg177[9]4.3Phe190Phe190MnP,Phe190TyrPhe190LeuPhe190IlePhe190Ala,MnP[17]wtMnPMnÒ[17]Phe190[17]Phe190MnP,IleAlaPhe190,Phe190Ala,MnPIÒ[17]pHPhe190,,,,pH,,MnP[1]SundaramoorthyM,KishiKGoldMH,etal.ThecrystalstructureofmanganeseperoxidasefromPhanerochaetechrysosporiumat2106!resolution.JBiolChem,1994,269,32759~32767[2]WariishiH,AkileswaranL,GoldMH.Manganeseperoxidasefrombasidiomycetephanerochaetechrysosporiumspectralcharacterzationoftheoxidizedstatesandthecatalyticcycle.Biochemistry,1988,27,5365~5370[3]SergeiL,Timofeevski,NieGuojun,etal.Reading,substratespecificityofligninperoxidaseandaS168Wvariantofmanganeseperoxidase.ArchBiochemBiophysics,2000,373,147~153[4]MinoY,WariishiH,BlackburnNJ,etal.,Spectralcharacterizationofmanganeseperoxidase,anextrocellularhemeenzymefromthelignin-degradingBasidiomycetePhanerochaetechrysosporium.JBiolChem.1988,263,7029~7036[5]MayfieldMB,GodfreyBJ,GoldMH,Characterizationofthemnp2geneencodingmanganeseperoxidaseisozyme2fromthebasidiomcetePhanerochaetechrysosporium.Gene,1994,142,231~235[6]SollewijnGelpkeMD,YoungHL,GoldMH.Effectsofcadmiumonmanganeseperoxidase:CompetitiveinhibitionofMn2+oxidationandthermalstabilizationoftheenzyme.EurJBiochem.,2000,267,1761~1769[7]SchullerDJ,BanN,HuysteeRB,etal.Structure,1996,4,311~321[8]HarrisRZ,WariishiH,GoldMH,etal.Thecatalyticsiteofmanganeseperoxidase.JBiolChem,1991,266:8751~8758[9]Roleofarginine177intheMnÒbindingsiteofmanganeseperoxidase:StudieswithR177D,R177E,R177N,andR177Qmutants,.EurJBiochem,2000,267,7038~7045[10]WhitwamR,TienM,HeterologousexpressionandreconstitutionoffungalMnperoxidase.ArchBiochemBiophys,1996,333,439~446[11]StewartP,WhitwamRE,KerstenPJ,etal.EfficientexpressionofaPhanerochaetechrysosporiummanganeseperoxidasegeneinAsergillusoryzae.ApplEnvironMicrobiol,1996,62,860~864[12]ConesaA,JeenesD,ArcherDB,Differentialregulationofmnp2,anewmanganeseperoxidase-encodinggenefromtheligninolyticfungusTrametesversicolorPRL572.ApplEnvirMicrobiol,2002,68:2077~2080[13]YoungsL,SundaramoorthyM,etal.CalnexinoverexpressionincreasesmanganeseperoxidaseproductioninAspergillusniger.ApplEnvirMicrobiol,2002,68,846~851[14]KishiK,Kusters-vansSM,MayfieldMB,etal.Characterzationofmanganese(Ò)bindingsitemutantsofmanganeseperoxidase.Biochemistry,1994,35,8986~8994[15]WhitwanRE,BrownKR,MusickM,etal.MutagenesisoftheMnÒ-bindingsiteofmanganeseperoxidaseaffectsxidationofMnÒbybothcompoundiandcompoundÒ.Biochemistry,1997,36,9766~9773[16]SollewijnGelpkeMD,MoÄnne-LoccozP.GoldMH,Arginine177isinvolvedinMn(Ò)bindingbymanganeseperoxidase.Biochemstry,1999,38,11481~11489[17]KishiK,HildebrandDP,Kusters-vanSomerenM,etal.Site-directedmutationsatPhe-190ofmanganeseperoxidase:Effectsonstability,function,andcoordination.Biochemistry,1997,36,4268~4277333:StructureandFunctionofManganesePeroxidaseHuMingLuXuemeiGaoPeiji(StateKeyLaboratoryofMicrobialTechnology,ShandongUniversityJinan250100)AbstractThearticlesummarizesthethree-dimensionalstructureandthecharacteristicsofcatalyticreactionsaboutmanganeseperoxidase,akeyenzymeinlignindegrading.Andtheresearchresultofthestructureandfunctionofmanganeseperoxidasethroughsite-directedmutationsetc.arereviewed.KeywordsMnperoxidasesite-directedmutationPhanerochaetechrysosporium,56,515,3,,,20031,,:33(1000