3.10.1.1: N-sulfoglucosamine sulfohydrolase
This is an abbreviated version!
For detailed information about N-sulfoglucosamine sulfohydrolase, go to the full flat file.
Word Map on EC 3.10.1.1
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3.10.1.1
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mucopolysaccharidosis
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lysosomal
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sanfilippo
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mps-iiia
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naglu
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n-sulfate
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sulfate-derived
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heparinum
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medicine
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oestrone
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hgsnat
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sumf1
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iduronate
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sulfatases
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ubiquitin-positive
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drug development
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pharmacology
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diagnostics
- 3.10.1.1
- mucopolysaccharidosis
- lysosomal
-
sanfilippo
-
mps-iiia
- naglu
-
n-sulfate
-
sulfate-derived
- heparinum
- medicine
- oestrone
- hgsnat
- sumf1
-
iduronate
-
sulfatases
-
ubiquitin-positive
- drug development
- pharmacology
- diagnostics
Reaction
Synonyms
2-desoxy-2-sulphamido-D-glucose sulphamidase, 2-desoxy-D-glucoside-2-sulphamate sulphohydrolase, heparan N-sulfatase, heparan-N-sulfatase, heparan-N-sulphatase, heparin sulfamidase, N-sulfoglucosamine sulfohydrolase, N-sulphoglucosamine, SGSH, sulfamate sulfohydrolase, sulfamidase, sulfoglucosamine sulfamidase, sulphamate sulphohydrolase, sulphamidase, sulphohydrolase
ECTree
3.10.1.1 N-sulfoglucosamine sulfohydrolaseAdvanced search results
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General Information on EC 3.10.1.1 - N-sulfoglucosamine sulfohydrolase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
despite the low sequence identity between the unique N-sulfatase and the group of O-sulfatases, they share a similar overall fold and active-site architecture, including a catalytic formylglycine, a divalent metal-binding site and a sulfate-binding site. A highly conserved lysine in O-sulfatases is replaced in the N-sulfoglucosamine sulfohydrolase by an arginine (Arg282) that is positioned to bind the N-linked sulfate substrate
malfunction
additional information
the enzyme shows low structural flexibility. The consensus active site lies in domain 1 in a narrow pocket at the bottom of a surface cleft and close to the end of the first beta-strand, active site structure, overview. Proposed interactions between the terminal N-sulfoglucosamine residue of the substrate with the enzyme in the active site
malfunction
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mutation S298P leads to 97.7% reduced enzyme activity and proteasomal degradation of the mutant enzyme causing the mild clinical phenotype of Sanfilippo A syndrome or Mucopolysaccharidosis type IIIA, a fatal inherited lysosomal storage disease accompanied by progressive neurologic degeneration, overview. PPatients are objects for early sulfamidase replacement therapy or treatment with selective pharmacological chaperones. Treatments with several pharmacological chaperones, such as nojirimycin, deoxygalactonojirimycin, deoxymannojirimycin, N-butyldeoxynojirimycin, phenylbutyric acid, at various concentrations do not increase the sulfamidase activity in S298P mutant expressing cells
malfunction
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deficient N-sulfoglucosamine sulfohydrolase enzyme activity causes mucopolysaccharidosis (MPS) type IIIA
malfunction
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deficient N-sulfoglucosamine sulfohydrolase enzyme activity causes mucopolysaccharidosis (MPS) type IIIA
malfunction
mucopolysaccharidoses are a group of recessively inherited lysosomal storage disorders caused by a deficiency of enzymes involved in the metabolic breakdown of glycosaminoglycans. Mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities, is caused by an inherited deficiency of the enzyme N-sulfoglucosamine sulfohydrolase, more than 100 mutations in the SGSH gene are found to reduce or eliminate its enzymatic activity. The Sanfilippo syndrome signs of neurodegeneration are the initial symptoms and comprise of hyperactivity, developmental stagnation and psychomotor regression
malfunction
mucopolysaccharidosis IIIA (MPS IIIA, Sanfilippo syndrome type A) is a lysosomal storage disorder caused by a deficiency of the enzyme heparan-N-sulfatase (EC 3.10.1.1), leading to accumulation of the glycosaminoglycan, heparan sulfate, in the lysosomes
malfunction
mucopolysaccharidosis type IIIA (MPS IIIA, Sanfilippo A) is a neurodegenerative lysosomal storage disorder caused by the deficiency of sulphamidase enzyme (SGSH) leading to accumulation of heparan sulfate
malfunction
mucopolysaccharidosis Type IIIA (MPSIIIA, Sanfilippo A syndrome), is an inherited neurodegenerative disease caused by mutations in the lysosomal enzyme, N-sulfoglucosamine sulfohydrolase. Mutations in the SGSH enzyme, the only mammalian heparan N-sulfatase, cause accumulation of lysosomal inclusion bodies in brain cells comprising heparan sulfate glycosaminoglycans. Systemic administration of MPSIIIA mice with the cTfRMAb-SGSH (IgG-SGSH fusion protein, where the IgG domain is a chimeric monoclonal antibody (mAb) against the mouse transferrin receptor (TfR)) fusion protein causes a 70% reduction in brain heparan sulfate, the pathologic glycosaminoglycan of the central nervous system in MPSIIIA
malfunction
Sanfilippo syndrome type A (mucopolysaccharidosis type IIIA) is a lysosomal disorder wherein deficient heparan-N-sulfatase (HNS) activity results in the accumulation of heparan sulfate in the central nervous system and is associated with progressive neurodegeneration in early childhood
malfunction
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deficient N-sulfoglucosamine sulfohydrolase enzyme activity causes mucopolysaccharidosis (MPS) type IIIA
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