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2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-D-glucose + H2O
?
-
-
-
?
aspartic acid beta-(4-nitroanilide) + H2O
4-nitroaniline + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
Thr-206 is the N-terminal nucleophile that acts as catalytic residue, Thr-206 is stabilized by hydrogen bonds from Ser-72 and Thr-224, enzyme structure
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-
?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
L-asparagine + H2O
L-aspartate + NH3
-
21% activity compared to N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine as substrate
-
r
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
L-aspartic acid-b-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
-
?
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
2-acetamido-2-deoxy-beta-D-glucopyranosylamine + L-asparagine
-
catalyzes the hydrolysis of the N-glycosylic bond
-
-
?
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
?
-
catabolism of N-linked oligosaccharides
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
N-acetyl-beta-D-glucosaminylamine + L-aspartate
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine, mechanism involving formation of a tetra-hedral high-energy intermediate, presence of a second binding site that may recognize substituted acetamido groups
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-
?
additional information
?
-
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
complex enzyme system in tissue homogenates
-
?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
7-amino-4-methylcoumarin + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
r
additional information
?
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview
-
-
?
additional information
?
-
-
processing and activation of aspartylglucosaminidase by autocatalytic cleavage, overview
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine in the catabolism of N-linked glycoproteins
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of a variety of asparagine and aspartyl compounds containing a free alpha-carboxyl group and a free alpha-amino group, study of enzyme specificity with 14 substrate analogues where the structure of the aspartyl group is changed, the alpha-carboxyl group is necessary for enzyme activity, but not the alpha-amino group, whose position acts as an anchor in the binding site for the substrate, no substrate: N-acetyl-D-glucosamine, intramolecular autoproteolytic activation reaction
-
-
?
additional information
?
-
-
enzyme level in plasma is elevated in congenital disorders of glycosylation type I, CDG I, a defect in biosynthesis or processing of O-linked glycans, overview
-
-
?
additional information
?
-
-
glycosylasparaginase hydrolyzes the N-glycosidic carbohydrate-to-protein linkage region, aspartylglucosamine, to L-aspartic acid and L-amino-N-acetylglucosamine through a reaction mechanism similar to L-asparaginase
-
-
?
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N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
N-acetyl-D-glucosaminylamine + L-aspartate
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
21% activity compared to N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine as substrate
-
r
N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O
?
-
catabolism of N-linked oligosaccharides
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
additional information
?
-
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
-
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
?
N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O
2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate
-
involved in degradation of glycoproteins
-
r
additional information
?
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population
-
-
?
additional information
?
-
-
enzyme catalyzes the hydrolysis of the N-glycosylic bond between asparagine and N-acetylglucosamine in the catabolism of N-linked glycoproteins
-
-
?
additional information
?
-
-
enzyme level in plasma is elevated in congenital disorders of glycosylation type I, CDG I, a defect in biosynthesis or processing of O-linked glycans, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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amidase deficiency
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Anemia, Sickle Cell
Gardos pathway to sickle cell therapies?
Aspartylglucosaminuria
A fluorometric assay for glycosylasparaginase activity and detection of aspartylglycosaminuria.
Aspartylglucosaminuria
A mouse model for the human lysosomal disease aspartylglycosaminuria.
Aspartylglucosaminuria
A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase.
Aspartylglucosaminuria
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Aspartylglucosaminuria
Amlexanox provides a potential therapy for nonsense mutations in the lysosomal storage disorder Aspartylglucosaminuria.
Aspartylglucosaminuria
Applications of a new fluorimetric enzyme assay for the diagnosis of aspartylglucosaminuria.
Aspartylglucosaminuria
Aspartylglucosaminidase (AGA) is efficiently produced and endocytosed by glial cells: implication for the therapy of a lysosomal storage disorder.
Aspartylglucosaminuria
Aspartylglucosaminuria (AGU): protein and gene structure of normal and mutated aspartylglucosaminidase.
Aspartylglucosaminuria
Aspartylglucosaminuria among Palestinian Arabs.
Aspartylglucosaminuria
Aspartylglucosaminuria caused by a novel homozygous mutation in the AGA gene was identified by an exome-first approach in a patient from Japan.
Aspartylglucosaminuria
Aspartylglucosaminuria in a Canadian family.
Aspartylglucosaminuria
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.
Aspartylglucosaminuria
Aspartylglucosaminuria: deficiency of aspartylglucosaminidase in cultured fibroblasts of patients and their heterozygous parents.
Aspartylglucosaminuria
Aspartylglucosaminuria: Unusual Neonatal Presentation in Qatari Twins With a Novel Aspartylglucosaminidase Gene Mutation and 3 New Cases in a Turkish Family.
Aspartylglucosaminuria
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.
Aspartylglucosaminuria
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Aspartylglucosaminuria
Assignment of the aspartylglucosaminidase gene (AGA) to 4q33----q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.
Aspartylglucosaminuria
Bilateral pulvinar signal intensity decrease on T2-weighted images in patients with aspartylglucosaminuria.
Aspartylglucosaminuria
Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.
Aspartylglucosaminuria
Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.
Aspartylglucosaminuria
Brain MRI findings in two Turkish pediatric patients with aspartylglucosaminuria.
Aspartylglucosaminuria
Characterization of a point mutation in aspartylglucosaminidase gene: evidence for a readthrough of a translational stop codon.
Aspartylglucosaminuria
Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.
Aspartylglucosaminuria
Characterization of the storage material of peripheral lymphocytes in aspartylglycosaminuria.
Aspartylglucosaminuria
Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.
Aspartylglucosaminuria
Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.
Aspartylglucosaminuria
Convenient and quantitative determination of the frequency of a mutant allele using solid-phase minisequencing: application to aspartylglucosaminuria in Finland.
Aspartylglucosaminuria
Correction of deficient enzyme activity in a lysosomal storage disease, aspartylglucosaminuria, by enzyme replacement and retroviral gene transfer.
Aspartylglucosaminuria
Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient.
Aspartylglucosaminuria
Deletion of the 3'-untranslated region of aspartylglucosaminidase mRNA results in a lysosomal accumulation disease.
Aspartylglucosaminuria
Deletion of the C-terminal end of aspartylglucosaminidase resulting in a lysosomal accumulation disease: evidence for a unique genomic rearrangement.
Aspartylglucosaminuria
Dissection of the molecular consequences of a double mutation causing a human lysosomal disease.
Aspartylglucosaminuria
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Aspartylglucosaminuria
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Aspartylglucosaminuria
Enzymatic diagnosis of aspartylglycosaminuria by fluorometric assay of glycosylasparaginase in serum, plasma, or lymphocytes.
Aspartylglucosaminuria
Enzyme replacement therapy in a mouse model of aspartylglycosaminuria.
Aspartylglucosaminuria
Expression and endocytosis of lysosomal aspartylglucosaminidase in mouse primary neurons.
Aspartylglucosaminuria
Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients.
Aspartylglucosaminuria
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Aspartylglucosaminuria
Genomic structure of human lysosomal glycosylasparaginase.
Aspartylglucosaminuria
Glycoasparaginase in human urine.
Aspartylglucosaminuria
Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts.
Aspartylglucosaminuria
Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria.
Aspartylglucosaminuria
Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.
Aspartylglucosaminuria
Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria.
Aspartylglucosaminuria
Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides.
Aspartylglucosaminuria
Isolation of the liver N-aspartyl-beta-glucosaminidase in aspartylglucosaminuria.
Aspartylglucosaminuria
Large-scale purification and preliminary x-ray diffraction studies of human aspartylglucosaminidase.
Aspartylglucosaminuria
Large-scale purification of human aspartylglucosaminidase: utilization of exceptional sodium dodecyl sulfate resistance.
Aspartylglucosaminuria
Linkage of aspartylglucosaminuria (AGU) to marker loci on the long arm of chromosome 4.
Aspartylglucosaminuria
Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria.
Aspartylglucosaminuria
Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.
Aspartylglucosaminuria
Massive accumulation of Man2GlcNAc2-Asn in nonneuronal tissues of glycosylasparaginase-deficient mice and its removal by enzyme replacement therapy.
Aspartylglucosaminuria
Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.
Aspartylglucosaminuria
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
Aspartylglucosaminuria
Monitoring the CNS pathology in aspartylglucosaminuria mice.
Aspartylglucosaminuria
Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuria.
Aspartylglucosaminuria
Phenotypic characterization of mice with targeted disruption of glycosylasparaginase gene: a mouse model for aspartylglycosaminuria.
Aspartylglucosaminuria
Pre-clinical Gene Therapy with AAV9/AGA in Aspartylglucosaminuria Mice Provides Evidence for Clinical Translation.
Aspartylglucosaminuria
Progressive neurodegeneration in aspartylglycosaminuria mice.
Aspartylglucosaminuria
Recombinant glycosylasparaginase and in vitro correction of aspartylglycosaminuria.
Aspartylglucosaminuria
Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.
Aspartylglucosaminuria
Single base deletion in exon 7 of the glycosylasparaginase gene causes a mild form of aspartylglycosaminuria in a patient of Mauritian origin.
Aspartylglucosaminuria
Spectrum of mutations in aspartylglucosaminuria.
Aspartylglucosaminuria
Splicing defect of the glycoasparaginase gene in two Japanese siblings with apartylglucosaminuria.
Aspartylglucosaminuria
Structural basis of aspartylglucosaminuria.
Aspartylglucosaminuria
Studies on N-aspartyl-beta-glucosaminidase in aspartylglycosaminuria.
Aspartylglucosaminuria
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Aspartylglucosaminuria
Toward understanding the neuronal pathogenesis of aspartylglucosaminuria: expression of aspartylglucosaminidase in brain during development.
Aspartylglucosaminuria
Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Aspartylglucosaminuria
Use of nonviral promoters in adenovirus-mediated gene therapy: reduction of lysosomal storage in the aspartylglucosaminuria mouse.
Aspartylglucosaminuria
[Molecular analysis of the aspartylglucosaminidase gene in Japanese patients with aspartylglucosaminuria]
Aspartylglucosaminuria
[Skeletal changes in 2 German children with aspartylglycosaminuria]
Congenital Disorders of Glycosylation
Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Cystic Fibrosis
Gene therapy to human diseases.
Genetic Diseases, Inborn
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Herpes Simplex
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Influenza, Human
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Intellectual Disability
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Intellectual Disability
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Intellectual Disability
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Intellectual Disability
Toward understanding the neuronal pathogenesis of aspartylglucosaminuria: expression of aspartylglucosaminidase in brain during development.
Leukemia
Depletion of L-asparagine supply and apoptosis of leukemia cells induced by human glycosylasparaginase.
Lysosomal Storage Diseases
Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.
Lysosomal Storage Diseases
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.
Lysosomal Storage Diseases
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Lysosomal Storage Diseases
Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.
Lysosomal Storage Diseases
Characterization of a point mutation in aspartylglucosaminidase gene: evidence for a readthrough of a translational stop codon.
Lysosomal Storage Diseases
Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.
Lysosomal Storage Diseases
Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.
Lysosomal Storage Diseases
Deletion of the 3'-untranslated region of aspartylglucosaminidase mRNA results in a lysosomal accumulation disease.
Lysosomal Storage Diseases
Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.
Lysosomal Storage Diseases
Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice.
Lysosomal Storage Diseases
Expression and endocytosis of lysosomal aspartylglucosaminidase in mouse primary neurons.
Lysosomal Storage Diseases
Fibroblast expression of collagens and proteoglycans is altered in aspartylglucosaminuria, a lysosomal storage disease.
Lysosomal Storage Diseases
Gene therapy to human diseases.
Lysosomal Storage Diseases
Genomic structure of human lysosomal glycosylasparaginase.
Lysosomal Storage Diseases
Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria.
Lysosomal Storage Diseases
Large-scale purification of human aspartylglucosaminidase: utilization of exceptional sodium dodecyl sulfate resistance.
Lysosomal Storage Diseases
Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients.
Lysosomal Storage Diseases
Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.
Lysosomal Storage Diseases
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
Lysosomal Storage Diseases
Pre-clinical Gene Therapy with AAV9/AGA in Aspartylglucosaminuria Mice Provides Evidence for Clinical Translation.
Lysosomal Storage Diseases
Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.
Lysosomal Storage Diseases
Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Lysosomal Storage Diseases
Use of nonviral promoters in adenovirus-mediated gene therapy: reduction of lysosomal storage in the aspartylglucosaminuria mouse.
Mucolipidoses
Catabolism of N-glycosylprotein glycans: evidence for a degradation pathway of sialylglyco-asparagines resulting from the combined action of the lysosomal aspartylglucosaminidase and endo-N-acetyl-beta-D-glucosaminidase. A 400-MHz 1H-NMR study.
Mucolipidoses
Glycosylasparaginase as a marker enzyme in the detection of I-cell disease
Mucolipidoses
Glycosylasparaginase as a marker enzyme in the detection of I-cell disease.
n4-(beta-n-acetylglucosaminyl)-l-asparaginase deficiency
Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient.
n4-(beta-n-acetylglucosaminyl)-l-asparaginase deficiency
Homozygous NADH-methemoglobin reductase and aspartylglucosaminidase deficiencies in a moderately retarded Sicilian child.
n4-(beta-n-acetylglucosaminyl)-l-asparaginase deficiency
Splicing defect of the glycoasparaginase gene in two Japanese siblings with apartylglucosaminuria.
Parkinson Disease
Gene therapy to human diseases.
Rubella
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
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C140S
the substitution is the causative mutation for enzyme deficiency. In addition to preventing the disulfide bond formation between C140 and C156, the C140S substitution also causes destabilization of the unique/longer loop structure in the human sequence and thus prevent dimerization of GA essential for autoproteolytic activation
D200A
87% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D201A
93% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
D70A
44% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
G226A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
G258A
inactive mutant, study of folding, transport and catalytic kinetics of mutant AGA
K230A
86% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
L15R
naturally occuring L15R, mutating the signal sequence, causes aspartylglucosaminuria and affects translocation of aspartylglucosaminidase
N225A
45% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
R138Q
the single mutation does not affect either the enzyme's autoproteolysis or its hydrolase activity
R138Q/C140S
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU). Due to a founder effect, AGU incidence in Finland is unexcelled, with one major allele (denoted AGUFIN) found in 98% of the AGU patients. The AGUFIN allele carries the two concurrent substitutions R138Q andC140S
R161Q/C163S
naturally occuring mutation, the AGUFin-major mutation is a combination of two missense mutations, abolishing a disulfide bond and destabilizing the AGA structure. The pathogenic C163S substitution is always combined with a functionally neutral Arg161Gln substitution. Mutations in the AGA gene result in aspartylglucosaminuria (AGU, OMIM 208400), a lysosomal storage disorder that is characterized by progressive loss of intellectual capabilities and some skeletal abnormalities. AGU patients are born seemingly normal, but the progressive course of the disease manifests in, e.g. developmental delay, loss of speech and coarse facial features early in childhood. In adulthood, most AGU patients are severely retarded and require special care
S238A
40% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T257I
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T33A
48% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA
T33S
same activity as wild-type AGA
D205G
-
essential for activation by autocatalytic proteolytic processing
H124R
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
H124W
-
reduced dimerization of the precursor polypeptide, total secretion into the medium
N308D
-
less than 10% of wild-type activity, misprocessing of precursor
N38D
-
30% of wild-type activity, proper processing to its mature lysosomal form
R234A
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234L
-
nearly complete decrease of activity, misprocessing of precursor in ER
R234Q
-
nearly complete decrease of activity, misprocessing of precursor in ER
T224A
-
nearly complete decrease of activity
T224S
-
nearly complete decrease of activity
T310A
-
less than 10% of wild-type activity, more properly cleaved form than N308D
G172D
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU)
G172D
site-directed mutagenesis, the mutation causes a local conformational change, which in turn disrupts the requisite autoprocessing step to generate metabolically functional mature hydrolase
G203D
naturally occuring mutation in Canadian population, causing aspartylglucosaminuria (AGU)
G203D
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU)
G226D
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU)
G226D
naturally occuring mutation in Canadian population, causing aspartylglucosaminuria (AGU)
T122K
naturally occuring mutation in Canadian population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T122K
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU)
T203I
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T203I
site-directed mutagenesis, corresponds to mutation T234I, the replacement of the conserved threonine with an isoleucine has negative impacts on both KM and, to a greater extent, kcat of hydrolase activity, the mutant is almost inactive. Structure comparison of mutant T203I with the wild-type enzyme. Mutant T203I is capable of autoprotolysis. In the T203I-substrate complex model, all the previously identified substrate binding residues (W11, F13, S50, T152, R180, D183, G204, G206) are in close contact distances from the substrate model, except the mutated residue Ile203
T234I
naturally occuring mutation in Canadian population,located at the rim of the substrate binding site , causing aspartylglucosaminuria (AGU). The mutatnt enzyme shows reduced autoprocessing capability compared to wild-type
T234I
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T99K
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU), the mutant lacks the signal peptide
T99K
naturally occuring mutation in US-American population causing aspartylglucosaminuria (AGU). This T99K model enzyme still has autoprocessing capacity to generate a mature form, its amidase activity to digest glycoasparagines remains low. A molecular clamp capable of fixing local disorders at the dimer interface might be able to rescue the deficiency of this AGU variant. The mutant lacks the signal peptide, but shows relatively high amidase activity, about 75% compared to wild-type. T99K has its substratebinding site fully opened through autoproteolysis and is ready to accommodate the substrate NAcGlc-Asn
T257A
-
nearly complete decrease of activity
T257A
-
nearly complete decrease of activity, misprocessing of precursor in ER
additional information
aspartylglucosaminuria-causing mutations, most of them lead to defective molecular maturation of AGA, effects of targeted amino acid substitutions on the activation process of AGA
additional information
-
aspartylglucosaminuria-causing mutations, most of them lead to defective molecular maturation of AGA, effects of targeted amino acid substitutions on the activation process of AGA
additional information
construction of a model enzyme corresponding to a Finnish AGU allele, the naturally occuring T234I mutant variant. The Finnish variant is capable of a slow autoprocessing to generate detectible hydrolyzation activity of the natural substrate of the enzyme. Determination of a 1.6 A-resolution structure of the Finnish AGU model and construction of an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on Km and kcat of the mature enzyme, overview
additional information
single nucleotide polymorphism rs2228119 (NM_000027.3:c.446C>G - p.(Thr149Ser)) results in amino acid variation Ser vs. Thr at position 149 (base and amino acid variation in red) of the human AGA enzyme. Functional analysis of the Ser149/Thr149 variants of human aspartylglucosaminidase and optimization of the coding sequence for protein production. Codon-optimized versions of the two variants are expressed at significantly higher levels than AGA with the natural codon-usage. The second most common allele in Finland is a 2 bp deletion called AGUFin-minor (NM_000027.3; c.199_200del - p.Glu67fc*3). Genotype frequency of single nucleotide polymorphism (SNP) rs2228119 in various populations
additional information
-
single nucleotide polymorphism rs2228119 (NM_000027.3:c.446C>G - p.(Thr149Ser)) results in amino acid variation Ser vs. Thr at position 149 (base and amino acid variation in red) of the human AGA enzyme. Functional analysis of the Ser149/Thr149 variants of human aspartylglucosaminidase and optimization of the coding sequence for protein production. Codon-optimized versions of the two variants are expressed at significantly higher levels than AGA with the natural codon-usage. The second most common allele in Finland is a 2 bp deletion called AGUFin-minor (NM_000027.3; c.199_200del - p.Glu67fc*3). Genotype frequency of single nucleotide polymorphism (SNP) rs2228119 in various populations
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