OMIMOnlineMendelianInheritanceinManAll DatabasesPubMedNucleotideProteinGenomeStructurePMCTaxonomyOMIM SearchPubMedProteinNucleotideCoreNucleotideGSSESTStructureGenomeBooksCancerChromosomesConservedDomainsdbGaP3DDomainsGeneGenomeProjectGENSATGEOProfilesGEODataSetsHomoloGeneJournalsMeSHNCBIWebSiteNLMCatalogOMIAOMIMPMCPopSetProbeProteinClustersPubChemBioAssayPubChemCompoundPubChemSubstanceSNPTaxonomyToolKitUniGeneUniSTSLimitsPreview/IndexHistoryClipboardDetailsDisplayTitlesDetailedClinicalSynopsisAllelicVariantsASN1XMLLinkOutRelatedEntriesBookLinksGeneLinksGenomeLinksGEOProfileLinksHomoloGeneLinksNucleotideLinksOMIALinksPubChemBioAssayLinksPMCLinksProteinLinksPubMed(calculated)LinksPubMed(cited)LinksSNPLinksGeneGenotypeLinksStructureLinksUniGeneLinksUniSTSLinksShow5102050100200500SendtoTextFilePrinterClipboardAll1OMIMdbSNP0OMIMUniSTS0+208400GeneTestsLinksASPARTYLGLUCOSAMINURIAAlternativetitlessymbolsAGUGLYCOSYLASPARAGINASEDEFICIENCYASPARTYLGLUCOSAMINIDASEDEFICIENCYAGADEFICIENCYGLYCOASPARAGINASEASPARTYLGLYCOSAMINURIAASPARTYLGLUCOSAMINIDASEINCLUDEDAGAINCLUDEDGenemaplocus4q32q33TEXTAspartylglucosaminuriaisalysosomaldiseasecausedbydeficiencyofNaspartylbetaglucosaminidaseItwasfirstreportedbyJennerandPollitt(1967)andPollittetal(1968)whofoundurinaryexcretionofabnormalamountsof2acetamido1(betaLaspartamido)12dideoxyglucoseina32yearoldfemaleandher20yearoldbrotherwithmentalretardationAnenzymeresponsibleforhydrolyzingthiscompoundisnormallypresentinseminalfluidbutwasabsentinthatofthebrotherAgeneralizedlackofthisenzymewaspostulatedBothsibshadthicksaggingskinofthecheeksafindingnotpresentinnormalmembersofthefamilyPaloandMattsson(1970)reported11casesTheparentsof1patientwerefirstcousinsTheyestimatedthatthereareatleast130casesinthetotalpopulationof45millioninFinlandTheFinnishcasesshowedinadditiontoseverementalretardationsaggingcheeksbroadnoseandfaceshortneckcranialasymmetryscoliosisperiodichyperactivityandvacuolatedlymphocytesDiarrheaandfrequentinfectionswereproblemsininfancyPKU(261600)hasaverylowincidenceinFinland(Palo1967)AGUisinFinlandwhatPKUisinmanyotherpopulationsAspartylglucosaminuriahasalsobeenobservedinFinnslivinginNorway(BorudandTorp1976)Autio(1980)estimatedthefrequencyat1in26000inFinlandAtotalof128casesin97familieshadbeenidentifiedMononenetal(1991)foundafrequencyof1in3643inastudyofchildrenineasternFinlandThisfrequencyisconsistentwithacarrierrateof1in30andindicatesthatthisdisorderaftertrisomy21andthefragileXsyndromeisthemostcommongeneticcauseofmentalretardationThedisorderreportedbyFountain(1974)wasshownnottobeaspartylglucosaminuriadespitesimilarities(Fountain1977)Indeedthatdisorderappearstorepresentadistinctautosomalrecessivedisorder(seeFountainsyndrome229120)Gehleretal(1981)describedaffectedbrotherandsisterinaconsanguineousItaliansibshiponeofthepatientsshowedangiokeratomacorporisdiffusumYoshidaetal(1991)andVargasDiezetal(2002)alsodescribedtheoccurrenceofangiokeratomacorporisdiffusumin2Japanesepatientsand1SpanishpatientrespectivelywithaspartylglucosaminuriaStevensonetal(1982)reportedthisdisorderinan18yearoldAmericanThefamilynamewasScottishIrishThemotherwassaidtohavebeenaged13yearsandthefatherwasunknowncircumstancessuggestingincestMentalretardationrecurrentinfectionscardiomyopathyandemotionallabilitywerefeaturesHreidarssonetal(1983)reportedacaseinanAmericanblackandanAmericanwhiteofuncertainparentageRadiographicchangesinthehandswerenotedthinepiphysesbroad'poorlymodeled'(undertubulated)metacarpalsandpeculiarlyshapedcarpalbonesIsenbergandSharp(1975)reportedthecaseofagirlofMexicanItalianextractionlivingintheUSMusumecietal(1984)reportedachildwithbothenzymopathicmethemoglobinemia(250800)andAGUSincethestructuralgenesfortheenzymesdeficientinthese2disordersareonseparatechromosomesasinglemutationsuchasasmalldeletionisnotlikelytobethebasisFurthermoreasibhadonlyAGUTheparentswereconsanguineousChitayatetal(1988)described3PuertoRicanbrotherswithfirstcousinparentswhohadAGUTwoofthebrothersweremonozygotictwinsMacroorchidismbecameevidentinall3boysatthetimeofpubertyThisfeaturehadnotpreviouslybeennotedinAGUalthoughotherendocrinologicabnormalitieshadbeendescribedYoshidaetal(1991)describedthefirstJapanesepatientswithAGUabrotherandsisteraged45and41respectivelyBothsibshadmentalretardationcoarsefacialfeaturesangiokeratomaandmyoclonicseizuresGordonetal(1998)describedaCanadianfamilyinwhich4of12sibswereaffected2brothersand2sistersThoughapparentlynormalatbirththeirdevelopmentalmilestonesparticularlyspeechwereslowandtheyacquiredonlyasimplevocabularyTherewasaprogressivecoarseningoffacialfeatures3hadinguinalherniaandrecurrentdiarrheaallbecameseverelyretardedandbythefourthdecadeshowedevidentdeteriorationofbothcognitiveandmotorskillsand2exhibitedcyclicbehavioralchangesThreeofthesibshaddiedat3339and44yearsofageAspartylglucosaminidase(AGAEC35126)isakeyenzymeinthecatabolismofNlinkedoligosaccharidesofglycoproteinsItcleavestheasparaginefromtheresidualNacetylglucosaminesasoneofthefinalstepsinthelysosomalbreakdownofglycoproteinsTheenzymeisalsoknownasglycoasparaginaseAGUistheonlyknownlysosomalstoragediseasecausedbyanamidasedeficiencyFisheretal(1990)clonedandsequencedacDNAfortheenzymedeficientinthisdisorderwhichtheyreferredtoasglycosylasparaginaseTollersrudandAronson(1989)purifiedglycosylasparaginasetohomogeneityfromratliverandfoundittohaveanativemolecularmassof49kDandtocomprise2subunitsof24and20kDFromstudyofacDNAforthehumanenzymeFisheretal(1990)foundthatitisencodedasa346kDpolypeptidethatisposttranslationallyprocessedtogenerate2subunitsofapproximately195(thealphasubunit)and15(thebetasubunit)kDIkonenetal(1991)clonedandsequencedafulllengthcDNAforhumanAGAandstudieditstransientexpressioninCOS1cellsByanalysisofsomaticcellhybridsAulaetal(1984)assignedthestructuralgeneforaspartylglucosaminidaseto4q21qterIn12AGUfamilieswith15affectedpersonsand50carriers(determinedbyreducedactivityofenzymeinlymphocytes)Gronetal(19891990)studiedlinkagetochromosome4markersandconcludedthatthelocusisdistaltoMNS(111300)TheysuggestedtheordercenADHEGFFGMNSAGUHalaletal(1991)presentedobservationstheyinterpretedasindicatinganarrowingoftheassignmentofthegeneto4q23q27agirlwithadenovodirecttandemduplicationof4q23q27hadincreasedactivityofAGAenzymeinculturedfibroblastsMorrisetal(1992)concludedfrominsituhybridizationstudiesthatthelocalizationis4q32q33Engelenetal(1992)foundreducedactivityoftheenzymeinapatientwithdeletionof4q33qterIkonenetal(1991)describedthespectrumof10AGUmutationsfoundin12unrelatedpatientsofnonFinnishoriginSince11ofthe12werehomozygotesconsanguinityappearstobeacommondenominatorinmostAGUfamiliesalthoughconsanguinitycouldbeconfirmedinonly2ofthefamiliesScreeningfortheunknowngenedefectswasdoneusingsinglestrandconformationpolymorphism(SSCP)analysisThemutationsweredistributedovertheentirecodingregionoftheAGUcDNAexceptinthecarboxylterminal17kDsubunitinwhichtheywereclusteredwithina46aminoacidregionBasedonthecharacterofthemutationsIkonenetal(1991)concludedthatmostofthemutationsprobablyaffectedthefoldingandstabilityofthemoleculeanddidnotdirectlyaffecttheactivesiteoftheenzymeTherewere3nonFinnishpatientswhohadthe'Finnish'cys163tosermutation(2084000001)but2ofthemwereNorwegianand1wasSwedishThesepatientspresumablyhadFinnishancestry(BorudandTorp1976)Tollersrudetal(1994)reportedon9patientsfrom7familiesidentifiedinnorthernNorwayAllwerehomozygousforthemostprevalentFinnishmutationcys163toserGenealogicinvestigationof9parentsprovedFinnishancestryinallpedigreesTheseFinnishimmigrantsoriginatedinthemainfromtheTorniovalleyinnorthernFinlandinacontinuousimmigrationmovementfrom1700to1900IkonenandPeltonen(1992)reviewedatotalof11AGUmutationspublishedtothattimeMononenetal(1994)describedafluorometricglycosylasparaginaseassayforneonatalscreeningforAGUOinonenetal(1995)determinedthehighresolutioncrystalstructureofhumanlysosomalaspartylglucosaminidaseTheenzymeissynthesizedasasinglepolypeptideprecursorthatisimmediatelyposttranslationallycleavedintoalphaandbetasubunitsTwoalphaandbetachainswerefoundtopacktogetherformingthefinalheterotetramericstructureThecatalyticallyessentialresiduetheNterminalthreonineofthebetachainissituatedinthedeeppocketofthefunnelshapedactivesiteOnthebasisofthestructureoftheenzymeproductcomplexOinonenetal(1995)presentedacatalyticmechanismforthislysosomalenzymewithanexceptionallyhighpHoptimumThe3dimensionalstructurealsoallowedthepredictionofthestructuralconsequencesofhumanmutationsresultinginaspartylglucosaminuriaLaitinenetal(1997)demonstratedthat2CanadiansibsofnonFinnishextractionhadAGUonthebasisofcompoundheterozygosityattheAGAlocusa299GAtransitioncausedagly100toglusubstitutionanda404TCtransitioncausedaphe135tosersubstitutionintheenzymeThecys163toser(C163S)mutationisresponsiblefor98%ofthecasesofAGUinFinlandIsoniemietal(1995)found7FinnishAGUpatientstobecompoundheterozygotesfortheC163Smutationandanothermutationnamelya2bpdeletioninthesecondexonoftheAGAcDNAcausingashiftofthereadingframeandaprematureterminationofthepolypeptidechainZlotogoraetal(1997)diagnosedthisdisorderin8patientsoriginatingfrom3unrelatedfamiliesallPalestinianArabsfromtheregionofJerusalemTheyfoundtheclinicaldiagnosisofAGUtobeoftendifficultinparticularearlyinthecourseofthediseaseandmostofthepatientswerediagnosedaftertheageof5yearsOntheotherhandsincethesepatientsexcreteearlylargeamountsofaspartylglucosamineinurinebiochemicaldetectioniseasybyurinechromatographyArvioetal(1999)studied66FinnishpatientswithAGUforchangesintheoralmucosaand44ofthoseforchangesinfacialskinNinepatientshadfacialangiofibromasEdemaofthebuccalmucosaandgingivalovergrowthsweremorefrequentinAGUpatientsthanincontrols(Plessthan0001)Of16oralmucosallesionsstudiedhistologically15representedfibroepithelialorepithelialhyperplasiasCytoplasmicvacuolizationwasevidentinonly4ExpressionofAGAinmucosallesionsofAGUpatientsdidnotdifferfromthatseenincorrespondinglesionsofnormalsubjectsArvioetal(2001)describedthestateofhealthintellectualskillsanddysmorphicfeaturesof19youngpatientswithaspartylglucosaminuriaOfthe195hadundergoneasuccessfulbonemarrowtransplantationbetween1991and1997Thefirst2patientswhoreceivedtransplantswereafter7and5years'followupmoreseverelymentallyretardedthanthenontransplantedpatientsThegeneralhealthofthelattergroupwasquitegoodwhereasthe5patientswhounderwentbonemarrowtransplantationhadposttransplantcomplicationsArvioetal(2001)concludedthatbonemarrowtransplantationshouldnotbeencouragedforthetreatmentofpatientswithaspartylglucosaminuriaafterinfancyNomenclatureSomeearlypublications(Autioetal1974BorudandTorp19761617Gehleretal19811981Maury1980)aswellassomerecentauthors(Kaartinenetal1996Mononenetal1994)usedthedesignationaspartylglycosaminuriaAspartylglucosaminuriaappearstobethemostwidelyuseddesignationSaarelaetal(2001)usedthe3dimensionalstructureofAGAtopredictstructuralconsequencesofAGUmutationsincluding6novelmutationsandtocharacterizetheeffectofmutationsonintracellularstabilitymaturationtransportandtheactivityofAGAMostmutationsaresubstitutionsreplacingtheoriginalaminoacidwithabulkierresidueMutationsofthedimerinterfacepreventdimerizationintheendoplasmicreticulumwhereasactivesitemutationsnotonlydestroytheactivitybutalsoaffectmaturationoftheprecursorDependingontheireffectsonthestabilityoftheAGApolypeptidetheauthorscategorizedmutationsasmildmoderateorsevereANIMALMODELTenhunenetal(1995)foundthattheAgageneinthemouseislocatedinthecentralareaoftheBregionofchromosome8intheregionthatshowshomologyofsyntenytothetelomericregionofhuman4qThemousegenespansan11kbgenomicregionandcontains9exonsand8intronswhichisanalogoustothehumangeneFurthermoretheexon/intronboundariesofthemouseandhumangenesareidenticallypositionedThroughtargeteddisruptionofthemouseAgageneinembryonicstemcellsKaartinenetal(1996)generatedmicethatcompletelylackAgaactivityAttheageof5to10monthsamassiveaccumulationofaspartylglucosaminewasdetectedinAganullmicealongwithlysosomalvacuolizationaxonalswellinginthegracilenucleusandimpairedneuromotorcoordinationAsignificantnumberofoldermalemicehadmassivelyswollenbladderswhichwasnotcausedbyobstructionbutwasmostlikelyrelatedtotheimpairedfunctionofthenervoussystemThefindingswereconsideredconsistentwiththepathogenesisofAGUandprovidedfurtherdataexplainingtheimpairedneurologicfunctioninAGUpatientsGonzalezGomezetal(1998)reportedthataftertheageof10monthsthegeneralconditionofthenullmutantmicecreatedbyKaartinenetal(1996)graduallydeterioratedTheysufferedfromprogressivemotorimpairmentandimpairedbladderfunctionanddiedprematurelyAwidespreadlysosomalhypertrophyinthecentralnervoussystemwasdetectedTheoldestanimals(20monthsold)displayedneuronallossandgliosisparticularlyintheregionswherethemostsevereneuronalvacuolationwasfoundThesevereataxicgaitoftheoldermicewasprobablyduetothedramaticlossofPurkinjecellsintensiveastrogliosisandvacuolationofneuronsinthedeepcerebellarnucleiandtheseverevacuolationofthecellsinvestibularandcochlearnucleiTheimpairedbladderfunctionandsubsequenthydronephrosisweresecondarytoinvolvementofthecentralnervoussystemThemicethusappearedtobeasuitableanimalmodelfortestingtherapeuticstrategiesinAGU(selectedexamples)0001ASPARTYLGLUCOSAMINURIAFINNISHTYPE[AGACYS163SER]BydirectsequencingofPCRamplifiedAGAcDNAfromanAGUpatientIkonenetal(1991)foundaGtoCmutationresultinginthesubstitutionofserineforcysteine163Thismutationwasfoundinallof20analyzedFinnishAGUpatientsandinheterozygousforminall53carriersandinnoneof67controlindividualsThemutationproducesachangeinthepredictedflexibilityoftheAGApolypeptidechainandremovesanintramolecularSSbridgeFisheretal(1991)independentlyfoundtheGtoCtransversioninDNAfromFinnishAGUfibroblastshowevertheyfoundasecondGtoAtransitionthatresultedinanargininetoglutaminesubstitutionaswellThe2substitutionswerepresentinall3Finnishcasesstudiedandinnoneof2nonFinnishAGUfibroblastlinesInnonFinnishAGUfibroblastsFisheretal(1991)founddeletionsastheapparentcauseoftheAGAdeficiencyMononenetal(1991)likewisefound2mutationsR161QandC163SBothmutationsresultedinnovelrestrictionendonucleasesitesandwerepresentinall8FinnishAGUpatientsstudiedbuttheywereabsentfromFinnishandnonFinnishcontrolsandanonFinnishcaseofAGUBothaminoacidchangeswouldbeexpectedtomodifythestructureoftheproteinprofoundlythereplacementofanargininebyglutaminerepresentsthesubstitutionofabasicaminoacidforonecontaininganunchargedpolargroupthereplacementofcysteinebyserinemayabolishadisulfidebridgeWhetherbothmutationsareinvolvedinthepathologicconsequencesorwhetheronemutationisapolymorphismwasuncertainIkonenetal(1991)showedbyinvitromutagenesisstudiesthatthecys163tosermutationisresponsibleforenzymedeficiencywhereasthearg161toglnsubstitutionwhichaccompaniestheothermutationin98%ofAGUallelesinFinlandrepresentsararepolymorphismCysteine163wasshowntoparticipateinanSSbridgeTheabsenceofthiscovalentcrosslinkinthemutatedproteinprobablyresultsindisturbedfoldingofthepolypeptidechainandconsequentdecreaseinitsintracellularstabilityFisherandAronson(1991)likewisefoundtheG482AtransitionandtheG488CtransversionanddemonstratedthatonlythelatterwasresponsiblefordeficiencyofglycosylasparaginaseactivityThesubstitutionpreventedthenormalposttranslationalprocessingoftheprecursorpolypeptideintoitsalphaandbetasubunits0002ASPARTYLGLUCOSAMINURIA[AGAGLY302ARG]Ina10yearoldTurkishchildwithAGUIkonenetal(1991)foundaGtoAsubstitutionatnucleotide904resultinginsubstitutionofarginineforglycine302ThepatientwashomozygousforthemutationandshowedfibroblastAGAactivityabout7%ofnormalTheparentswerefirstcousins0003ASPARTYLGLUCOSAMINURIA[AGACYS306ARG]Ina16yearoldAmericanwhitepatientIkonenetal(1991)foundbytheSSCPmethodaTtoCchangeatnucleotide916resultinginsubstitutionofarginineforcysteine3060004ASPARTYLGLUCOSAMINURIA[AGAGLY60ASP]Ina3yearoldGermanchildreportedbyZiegleretal(1989)Ikonenetal(1991)foundaGtoAsubstitutionatnucleotide179resultinginsubstitutionofthenegativelychargedasparticacidforunchargedglycineatresidue600005ASPARTYLGLUCOSAMINURIA[AGAALA101VAL]Ina1yearoldItalianchildIkonenetal(1991)foundaCtoTtransitionatnucleotide302thatchangedalanine101tovalineThepatientwashomozygousforthismutationwhichwasdiscoveredbytheSSCPmethodThesamemutationwasfoundinacompoundheterozygoteanEnglishpatient(see2084000006)0006ASPARTYLGLUCOSAMINURIA[AGA7BPDELNT102108DELFS34TER]Ina5yearoldEnglishchildIkonenetal(1991)foundcompoundheterozygosityfortheala101tovalmutationanda7nucleotidedeletion(nucleotides102108)Thegenedeletionwouldbepredictedtoresultintheformationofatruncatedpolypeptidechainofonly33aminoacids0007ASPARTYLGLUCOSAMINURIA[AGA1BPINSFS319TER]Ina17yearoldSpanishAmericanpatientIkonenetal(1991)foundinsertionofasinglethymidineafternucleotide800resultinginashiftinthereadingframeandaprematurestopcodoncausingatruncatedpolypeptidechainwith318aminoacidsofwhichthefirst267aminoacidsrepresentedthenormalAGApolypeptide0008ASPARTYLGLUCOSAMINURIA[AGA6BPINS]Ina3yearoldTunisianchildtheoffspringoffirstcousinparentsIkonenetal(1991)foundhomozygosityfora6nucleotideinsertion(ATGCGG)afternucleotide127causinganinframeinsertionofasparticacidandalanineafteraminoacid420009ASPARTYLGLUCOSAMINURIA[AGAIVS8GT+1]Ina12yearoldblackAmericanpatient(Hreidarssonetal1983CamdennumberGM03560)Ikonenetal(1991)foundhomozygosityforadeletionofnucleotides807940InthispatientfurthersequenceanalysisofbothcDNAandgenomicDNAconfirmedthata134bpexonwasmissingfromthecDNAandthataGtoTsubstitutionhadoccurredintheadjacent3primeintronatposition+1ofthesplicedonorsiteThusthiswasasplicingmutationThemutationresultedinatranscriptthatwas134bpshorterthannormalThemutationalsoresultedintheshiftofthereadingframeandaprematureterminationcodonatthebeginningofthefollowingexon0010ASPARTYLGLUCOSAMINURIA[AGA1BPDELFS127TER]Inan8yearoldDutchchildIkonenetal(1991)founddeletionof1nucleotidethymidine800Thisresultedinframeshiftandprematureterminationofthepolypeptidechainafter126aminoacids0011MOVEDTO20840000090012ASPARTYLGLUCOSAMINURIA[AGASER72PRO]Peltolaetal(1996)reportedthataTtoCchangeatcodon214leadingtoaser72toprosubstitutionoccurredinaffectedmembersin4ArabfamilieswithaspartylglucosaminuriaTheynotedthatthismutationisthefirstnaturallyoccurringAGAmutationthatinvolvesanactivesiteandisapparentlythesecondmostcommonAGAmutationworldwideSEEALSOAulaetal(1984)Aulaetal(1984)Ikonenetal(1991)Ikonenetal(1991)IsenbergandSharp(1976)Mononenetal(1992)Mononenetal(1991)REFERENCES1ArvioMSaunaahoOPeippoMBonemarrowtransplanationforaspartylglucosaminuriafollowupstudyoftransplantedandnontransplantedpatientsJPediat1382882902001PubMedID111746352ArvioPArvioMKeroMPirinenSLukinmaaPLOvergrowthoforalmucosaandfacialskinanovelfeatureofaspartylglucosaminuriaJMedGenet363984041999PubMedID103537873AulaPAstrinKHFranckeUDesnickRJAssignmentofthestructuralgeneencodinghumanaspartylglucosaminidasetothelongarmofchromosome4(4q214qter)(Abstract)AmJHumGenet36201Sonly19844AulaPAstrinKHFranckeUDesnickRJAssignmentofthestructuralgeneencodinghumanaspartylglucosaminidasetothelongarmofchromosome4(4q214qter)AmJHumGenet36121512241984PubMedID65170505AulaPRapolaJvonKoskullHAmmalaPPrenataldiagnosisandfetalpathologyofaspartylglucosaminuriaAmJMedGenet193593671984PubMedID65074826AutioSAspartylglucosaminuria(AGU)InErikssonAWForsiusHRNevanlinnaHRWorkmanPLNorioRKPopulationStructureandGeneticDisordersNewYorkAcademicPress(pub)1980Pp5775827AutioSPaloJPerheentupaJAspartylglycosaminuriaagargoylelikesyndromewithautosomalrecessiveinheritanceBirthDefectsOrigArtSerX(4)19320019748BorudOTorpKHAspartylglycosaminuriainnorthernNorway(Letter)LancetI1082108319769ChitayatDNakagawaSMarionRWSachsGSHahmSYEGoldmanHSAspartylglucosaminuriainaPuertoRicanfamilyadditionalfeaturesofapanethnicdisorderAmJMedGenet315275321988PubMedID322813610EngelenJHamersASchranderStumpelCMulderHPoorthuisBAssignmentoftheaspartylglucosaminidasegene(AGA)to4q33q35basedondecreasedactivityinagirlwitha46XXdel(4)(q33)karyotypeCytogenetCellGenet602082091992PubMedID150521711FisherKJAronsonNNJrCharacterizationofthemutationresponsibleforaspartylglucosaminuriainthreeFinnishpatientsaminoacidsubstitutioncys163toserabolishestheactivityoflysosomalglycosylasparaginaseanditsconversionintosubunitsJBiolChem26612105121131991PubMedID190487412FisherKJTollersrudOKAronsonNNJrMoleculargeneticsofaspartylglucosaminuria(Abstract)NucleicAcidsResSymp238only199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8745PollittRJJennerFAMerskeyHAspartylglycosaminuriaaninbornerrorofmetabolismassociatedwithmentaldefectLancetII253255196846SaarelaJLaineMOinonenCvonSchantzCJalankoARouvinenJPeltonenLMolecularpathogenesisofadiseasestructuralconsequencesofaspartylglucosaminuriamutationsHumMolecGenet109839952001PubMedID1130937147StevensonRETaylorHAWilkesGAspartylglucosaminuriaProcGreenwoodGenetCenter16972198248TenhunenKLaanMManninenTPalotieAPeltonenLJalankoAMolecularcloningchromosomalassignmentandexpressionofthemouseaspartylglucosaminidasegeneGenomics302442501995PubMedID858642349TollersrudOKAronsonNNJrPurificationandcharacterizationofratliverglycosylasparaginaseBiochemJ2601011081989PubMedID277517450TollersrudOKNilssenOTranebjaergLBorudOAspartylglucosaminuriainnorthernNorwayamolecularandgenealogicalstudyJMedGenet313603631994PubMedID806481151VargasDiezEChabasACollMJSanchezPerezJGarciaDiezAFernandezHerreraJMAngiokeratomacorporisdiffusuminaSpanishpatientwithaspartylglucosaminuriaBritJDerm1477607642002PubMedID1236642652YoshidaKIkedaSYanagisawaNYamauchiTTsujiSHirabayashiYTwoJapanesecaseswithaspartylglycosaminuriaclinicalandmorphologicalfeaturesClinGenet403183251991PubMedID175660453YoshidaKIkedaSYanagisawaNYamauchiTTsujiSHirabayashiYTwoJapanesecaseswithaspartylglycosaminuriaclinicalandmorphologicalfeaturesClinGenet403183251991PubMedID175660454ZieglerRSchmidtHSewellACWeglageJvLengerkeJHUllrichKAspartylglucosaminurieKlinischeBeschreibungvonzweideutschenPatientenMschrKinderheilk137454457198955ZlotogoraJBenNeriahZAbuLibdehBYSuryVZeiglerMAspartylglucosaminuriaamongPalestinianArabsJInheritMetabDis207998021997PubMedID9427148CONTRIBUTORSGaryABellusupdated4/11/2003GeorgeETillertiller10/2/2001AdaHamoshupdated4/23/2001MichaelJWrightupdated7/12/1999VictorAMcKusickupdated3/11/1999VictorAMcKusickupdated1/20/1999VictorAMcKusickupdated2/19/1998VictorAMcKusickupdated1/6/1998VictorAMcKusickupdated6/27/1997MoyraSmithupdated6/22/1996CREATIONDATEVictorAMcKusick6/3/1986EDITHISTORYcarol6/7/2005carol6/17/2004alopez3/17/2004alopez4/11/2003cwells10/10/2001cwells10/2/2001cwells5/9/2001cwells5/8/2001terry4/23/2001jlewis7/23/1999jlewis7/19/1999terry7/12/1999carol3/16/1999terry3/11/1999carol1/29/1999terry1/20/1999carol9/28/1998carol6/26/1998terry6/4/1998mark2/25/1998terry2/19/1998terry1/6/1998alopez7/3/1997jenny7/2/1997mark7/1/1997terry6/27/1997alopez6/10/1997carol6/24/1996carol6/23/1996carol6/22/1996mark1/14/1996mark12/6/1995terry8/30/1994davew8/17/1994jason6/16/1994mimadm4/18/1994warfield4/14/1994pfoster4/1/1994Copyright©19662007JohnsHopkinsUniversityDisplayTitlesDetailedClinicalSynopsisAllelicVariantsASN1XMLLinkOutRelatedEntriesBookLinksGeneLinksGenomeLinksGEOProfileLinksHomoloGeneLinksNucleotideLinksOMIALinksPubChemBioAssayLinksPMCLinksProteinLinksPubMed(calculated)LinksPubMed(cited)LinksSNPLinksGeneGenotypeLinksStructureLinksUniGeneLinksUniSTSLinksShow5102050100200500SendtoTextFilePrinterClipboardDisclaimerWritetotheHelpDeskPrivacyPolicyNCBINLMNIH