3.1.6.13: iduronate-2-sulfatase
This is an abbreviated version!
For detailed information about iduronate-2-sulfatase, go to the full flat file.
Word Map on EC 3.1.6.13
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3.1.6.13
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mucopolysaccharidosis
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lysosomal
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glycosaminoglycans
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x-linked
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dermatan
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heparan
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multisystemic
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sulfatases
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hepatosplenomegaly
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medicine
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arylsulfatase
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mpsii
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x-chromosome
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enzyme-replacement
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analysis
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synthesis
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alpha-l-iduronidase
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neuronopathic
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infusion-related
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drug development
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6-minute
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dysostosis
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diagnostics
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shire
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hurler
- 3.1.6.13
- mucopolysaccharidosis
- lysosomal
- glycosaminoglycans
-
x-linked
- dermatan
- heparan
-
multisystemic
-
sulfatases
-
hepatosplenomegaly
- medicine
- arylsulfatase
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mpsii
-
x-chromosome
-
enzyme-replacement
- analysis
- synthesis
- alpha-l-iduronidase
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neuronopathic
-
infusion-related
- drug development
-
6-minute
- dysostosis
- diagnostics
-
shire
- hurler
Reaction
Synonyms
2-sulfo-L-iduronate 2-sulfatase, chondroitinsulfatase, elaprase, Hunter corrective factor, I2S, IDS, IDS-Like, IDS-like enzyme, iduronate 2-sulfatase, iduronate 2-sulfate sulfatase-like, iduronate 2-sulfate-like enzyme, iduronate sulfatase, iduronate sulfate sulfatase, iduronate-2-sulfatase, iduronate-2-sulfate sulfatase, iduronate-2-sulphatase, iduronide-2-sulfate sulfatase, idurono-2-sulfatase, idursulfase, L-iduronate 2-sulfate sulfatase, L-idurono sulfate sulfatase, sulfatase, L-idurono-, sulfo-L-iduronate sulfatase, sulfoiduronate sulfohydrolase
ECTree
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Engineering
Engineering on EC 3.1.6.13 - iduronate-2-sulfatase
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A85T
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mutation identified in patient with mucopolysaccharidosis type II, attenuated phenotype. 1.2% residual activity, presence of both the precursor form and processed form of enzyme
C84S
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artificial mutation in predicted active site. No enzymic acitivity, presence of both the precursor form and processed form of enzyme
C84T
D148V
the mutation perturbs the structure or molecular interactions of the enzyme, leading to loss of enzyme activity and severe phenotype of disease
E254X
the mutation produces truncated protein lacking 54% of the IDS protein, which leads to severe clinical presentations
G140R
the mutant has 22% of the activity from cells expressing wild type IDS
K227E
the mutation perturbs the structure or molecular interactions of the enzyme, leading to loss of enzyme activity and severe phenotype of disease
L339P
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L339P is a mucopolysaccharidosis type II-causing mutation affecting maturation of the protein, the missense variant has stable mRNA but the residual enzyme activity remains 1.2% of wild type level
L339R
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the missense variant has stable mRNA but the residual enzyme activity remains 2.3% of wild type level
P86L
Q389X
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the nonsense mutation leads to premature chain termination at codom 398 and causes mucopolysaccharidosis type II
Q531X
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mutation identified in patient with mucopolysaccharidosis type II, attenuated phenotype. 2.4% residual activity, presence of a truncated 68000 Da protein form
R443X
the mutation produces truncated protein lacking 20% of the IDS protein, which leads to severe clinical presentations
R468L
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mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
R468Q
R468W
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mutations identified in Taiwanese patients with mucopolysaccharidosis type I, mutations R468Q and R468W together account for 48% of mutations found
R48P
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mutation identified in patient with mucopolysaccharidosis type II, attenuated phenotype. 0.33% residual activity, presence of both the precursor form and processed form of enzyme
S333L
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mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
S349I
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mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
S369X
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the nonsense mutation leads to premature chain termination at codom 369 and causes mucopolysaccharidosis type II
W337R
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mutation identified in patient with mucopolysaccharidosis type II, attenuated phenotype. 0.2% residual activity, presence of both the precursor form and processed form of enzyme
W337X
the mutation produces truncated protein lacking 39% of the IDS protein, which leads to severe clinical presentations
additional information
C84T
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artificial mutation in predicted active site. No enzymic acitivity, presence of both the precursor form and processed form of enzyme
P86L
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mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
P86L
the mutation activates multiple cryptic splice sites, resulting in aberrantly spliced transcripts of IDS
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mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
R468Q
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mutations identified in Taiwanese patients with mucopolysaccharidosis type I, mutations R468Q and R468W together account for 48% of mutations found
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in 25 Hunter syndrome patients 20 mutations of the gene are identified of which 13 mutations are novel
additional information
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K347T, N265I, 473delTCC, 533delTT mutations are identified in four out of 28 Hunter syndrome patients
additional information
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Q80X, R88C, c145-161del insT, D198G, c247delG, L259P, S333L, E341K, W345X, R468Q, P480R, R48P mutations are identified in Hunter syndrome patients
additional information
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R88H, R88P, T118I, 959delT, R468Q mutations are identified in Hunter syndrome patients
additional information
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analysis of enzyme gene in Portuguese patients with mucopolysaccharidosis type II. Splice mutations at the IDS locus account for almost 56% of cases. Mutations include six intronic splice mutations, c.104?2A>G, c.241?2A>G, c.241?1G>A, c.418+1G>A, c.880?8A>G and c.1181?1G>C, two exonic splice mutations, c.1006G>C and c.1122C>T, five missense mutations, D269V, D69V, D148N, R88C and P86L, one nonsense mutation, Q465Ter, one total IDS gene deletion, and one rearrangement involving a IDS gene inversion
additional information
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analysis of mutations identified in patients with mucopolysaccharidosis type II. Mutations lead to aberrant precursor forms and loss of normal maturation of precursor. Mutant enzymes exhibit 2-4% of wild-type activity
additional information
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characterization of three mucopolysaccharidosis II patients with multiple aberrant transcripts due to three different point mutations. Mutations lead to production of only abnormally spliced transcripts (c.418+1G>C) or to abnormally spliced transcripts in addition to correctly spliced transcripts bearing the respective missence mutation (c.419G>T, and c.245C>T)
additional information
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identification of 10 different mutations in Taiwanese patients with mucopolysaccharidosis type I, mutations R468Q and R468W together accounting for 48% of mutations found
additional information
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to deliver the enzyme across the human blood-brain barrier, the sulfatase is re-engineered as an IgG-sulfatase fusion protein with a genetically engineered monoclonal antibody against the human insulin receptor. The human insulin receptor monoclonal antibody HIRMAb part of the HIRMAb-IDS fusion protein acts as a molecular Trojan horse to ferry the fused IDS across the blood-brain barrier, overview. The HIRMAb-IDS fusion protein is tritiated and injected intravenously into the adult Rhesus monkey at a low dose of 0.1 mg/kg. The IDS enzyme activity in plasma is elevated 10fold above the endogenous level, and therapeutic plasma concentrations are generated in vivo. The uptake of the HIRMAb-IDS fusion protein in the brain is sufficiently high to produce therapeutic concentrations of IDS in the brain following IV administration of the fusion protein
additional information
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in 25 Hunter syndrome patients 20 mutations of the gene are identified of which 13 mutations are novel