@prefix activity: .
@prefix address: .
@prefix agency: .
@prefix assay: .
@prefix assayCategory: .
@prefix assayTargetLink: .
@prefix biopax3: .
@prefix calbc: .
@prefix calbc-group: .
@prefix carrierLink: .
@prefix certainAgreement: .
@prefix chebi: .
@prefix chembl: .
@prefix chemicalCompound: .
@prefix chemicalCompoundRecord: .
@prefix clan: .
@prefix clinicalResult: .
@prefix clinicalStudy: .
@prefix clinicaltrials: .
@prefix company: .
@prefix confidenceScore: .
@prefix contact: .
@prefix country: .
@prefix cpath: .
@prefix curationLookup: .
@prefix dailymed: .
@prefix dailymed-drugs: .
@prefix dailymed-ingredient: .
@prefix dailymed-instance: .
@prefix databaseReference: .
@prefix dc: .
@prefix dc-term: .
@prefix diseaseontology: .
@prefix diseasome: .
@prefix diseasome-diseases: .
@prefix diseasome-gene: .
@prefix diseasome-instance: .
@prefix documentType: .
@prefix dosageForm: .
@prefix drug: .
@prefix drugbank: .
@prefix drugbank-proteinSequence: .
@prefix drugCategory: .
@prefix drugInteraction: .
@prefix drugTarget: .
@prefix eligibility: .
@prefix entrez-gene: .
@prefix entrez-goterm: .
@prefix entrezgene: .
@prefix enzymeLink: .
@prefix externalIdentifier: .
@prefix externalLink: .
@prefix factforge: .
@prefix family: .
@prefix foaf: .
@prefix formulation: .
@prefix freebase: .
@prefix gene-rif: .
@prefix geneontology: .
@prefix geneSequence: .
@prefix hapmap: .
@prefix indication: .
@prefix intervention: .
@prefix investigator: .
@prefix label: .
@prefix lhgdn: .
@prefix lifeskim: .
@prefix linkedct: .
@prefix linkedct-condition: .
@prefix linkedct-intervention: .
@prefix literatureCitation: .
@prefix lld: .
@prefix location: .
@prefix measurement: .
@prefix meddraSideEffect: .
@prefix mixture: .
@prefix molecularSpecies: .
@prefix molecule: .
@prefix moleculeType: .
@prefix ontotext: .
@prefix organismSpecies: .
@prefix outcomeAnalysis: .
@prefix outcomeMeasure: .
@prefix overallOfficial: .
@prefix owl: .
@prefix owlim: .
@prefix packager: .
@prefix participantFlow: .
@prefix patent: .
@prefix pfam: .
@prefix phenotype: .
@prefix pointOfContact: .
@prefix price: .
@prefix primaryOutcome: .
@prefix product: .
@prefix property: .
@prefix proteinSequence: .
@prefix pubmed: .
@prefix pubmed-article: .
@prefix pubmed-author: .
@prefix pubmed-mesh: .
@prefix pubmed-meshheading: .
@prefix pubmed-qualifier: .
@prefix rdf: .
@prefix rdfs: .
@prefix relationshipType: .
@prefix relontology: .
@prefix reportingGroup: .
@prefix researchStem: .
@prefix responsibleParty: .
@prefix result: .
@prefix resultsBaseline: .
@prefix resultsMeasure: .
@prefix resultsOutcome: .
@prefix secondaryOutcome: .
@prefix sideEffect: .
@prefix sideEffectFrequency: .
@prefix sider: .
@prefix sider-drug: .
@prefix skos: .
@prefix skos-xl: .
@prefix snp: .
@prefix structureType: .
@prefix studyMilestone: .
@prefix studyParticipants: .
@prefix studyPeriod: .
@prefix substructure: .
@prefix symptom: .
@prefix synonym: .
@prefix targetLink: .
@prefix targetType: .
@prefix taxonomy: .
@prefix taxonomyClass: .
@prefix taxonomyKingdom: .
@prefix transporterLink: .
@prefix umls: .
@prefix umls-concept: .
@prefix umls-label: .
@prefix umls-semnetwork: .
@prefix uniprot: .
@prefix uniprot-protein: .
@prefix uniprot-unstable: .
@prefix xsd: .
pubmed-article:8280063 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0086418 , umls-concept:C0001044 , umls-concept:C0441655 , umls-concept:C1280500 , umls-concept:C0220781 , umls-concept:C0205360 ;
pubmed:dateCreated "1994-2-7" ;
pubmed:abstractText "The role of N-glycosylation in the function of human acetylcholinesterase (HuAChE) was examined by site-directed mutagenesis (Asn to Gln substitution) of the three potential N-glycosylation sites Asn-265, Asn-350 and Asn-464. Analysis of HuAChE mutants, defective in a single or multiple N-glycosylation sites, by expression in transiently or stably transfected human embryonal 293 kidney cells suggests the following. (a) All three AChE glycosylation signals are utilized, but not all the secreted molecules are fully glycosylated. (b) Glycosylation at all sites is important for effective biosynthesis and secretion; extracellular AChE levels in mutants defective in one, two or all three sites amounted to 20-30%, 2-4% and about 0.5% of wild-type level respectively. (c) Some glycosylation mutants display impaired stability, as reflected by increased susceptibility to heat inactivation; substitution of Asn-464 has the most pronounced effect on thermostability. (d) Abrogation of N-glycosylation has no detectable effect on the enzyme activity of HuAChE; all glycosylation mutants, including the triple mutant, hydrolyse acetylthiocholine efficiently, displaying Km, kcat. and kcat./Km values similar to those of the wild-type enzyme. (e) In most mutants, inhibition profiles with edrophonium and bisquaternary ammonium ligands are identical with those of wild-type enzyme; the Asn-350 mutants, however, exhibit a slight decrease in their affinity towards these ligands. (f) Elimination of oligosaccharide side chains has no detectable effect on the surface-related 'peripheral-site' functions; like the wild-type enzyme, all mutants were inhibited by propidium and by increased concentrations of acetylthiocholine." ;
pubmed:commentsCorrections , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , , , , ;
pubmed:status "MEDLINE" ;
pubmed:month "Dec" ;
pubmed:issn "0264-6021" ;
pubmed:author pubmed-author:CohenSS , pubmed-author:ShaffermanAA , pubmed-author:LeitnerMM , pubmed-author:VelanBB , pubmed-author:FlashnerYY , pubmed-author:KronmanCC , pubmed-author:OrdentlichAA ;
pubmed:issnType "Print" ;
pubmed:day "15" ;
pubmed:volume "296 ( Pt 3)" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "649-56" ;
pubmed:dateRevised "2009-11-18" ;
pubmed:meshHeading pubmed-meshheading:8280063-Humans , , pubmed-meshheading:8280063-Mutation , pubmed-meshheading:8280063-Catalysis , , , pubmed-meshheading:8280063-Glycosylation , , pubmed-meshheading:8280063-Oligosaccharides , pubmed-meshheading:8280063-Acetylcholinesterase , , pubmed-meshheading:8280063-Edrophonium , , pubmed-meshheading:8280063-Transfection , ;
pubmed:year "1993" ;
pubmed:articleTitle "N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis." ;
pubmed:affiliation "Department of Biochemistry, Israel Institute for Biological Research, Ness-Ziona." ;
pubmed:publicationType "Journal Article" , "Research Support, U.S. Gov't, Non-P.H.S." .