3.1.6.13: iduronate-2-sulfatase
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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
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x-linked
- dermatan
- heparan
-
multisystemic
-
sulfatases
-
hepatosplenomegaly
- medicine
- arylsulfatase
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mpsii
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x-chromosome
-
enzyme-replacement
- analysis
- synthesis
- alpha-l-iduronidase
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neuronopathic
-
infusion-related
- drug development
-
6-minute
- dysostosis
- diagnostics
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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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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
direct assay for enzyme activity using substrate 4-methylumbelliferyl alpha-L-idopyranosiduronic acid 2-sulfate and LC-MS/MS based detection
drug development
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HIRMAb-IDS fusion protein is a bifunctional IgG-sulfatase fusion protein, specifically engineered for targeted drug delivery across the human blood-brain barrier
medicine
synthesis
additional information
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improvement of the total activity of recombinant IDS-Like at 3 litre bioreactor in glycerol as carbon source. Clone IDS28 of Pichia pastoris expressing IDS-Like employed for low-scale production of the recombinant enzyme in a saline culture media without phosphate. Biological activity is about 1.73 to 7times higher in batch culture than the result obtained with the same clone in shake flask culture
medicine
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deficiency in Hunters syndrome, mucopolysaccharidosis II
medicine
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in humans, the inherited deficiency of the enzyme activity results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
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in humans, the inherited deficiency of the enzyme activity results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
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the inherited deficiency results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
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the inherited deficiency results in mucopolysaccharidosis type II, the Hunter syndrome, studies of transfer of the recombinant enzyme into brain cells in vitro
medicine
monoclonal antibodies demonstrate the capacity to differentiate progressive structural changes in iduronate-2-sulphatase and can be used to characterize the severity of mucopolysaccharidosis type II in patients based on variable denatured microstates
medicine
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analysis of 11 patients with mutations in the IDS gene leading to mucopolysaccharidosis type II. Structural alteration in the IDS protein results in its rapid degradation and/or insufficiency in processing
medicine
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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
medicine
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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)
medicine
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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. Due to overlapping significant wide range of enzyme activity in normal controls and in carriers of mutations, the level of enzyme activity cannot be used alone for carrier detection
medicine
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cognitive involvement is indicative of more severe disease and lower life expectancy in patients with mucopolysaccharidosis type II caused by a deficiency of iduronate-2-sulfatase: median age at death is significantly lower in patients who died in or before 1985 compared with those who died after 1985. Data from patients who died after 1985 may serve as a control in analyses of the effects of enzyme replacement therapy with idursulfase on mortality in patients with mucopolysaccharidosis type II. Idursulfase does not cross the blood-brain barrier in therapeutic quantities
medicine
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early treatment of mucopolysaccharidosis type II mice with one systemic injection of AAV2/5CMV-hIDS results in prolonged and high levels of circulating IDS that can efficiently and simultaneously rescue both visceral and central nervous system defects for up to 18 months after therapy
medicine
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efficacy of cord blood stem cell transplantation for Hunter disease (deficiency of IDS) is judged to be insufficient for the brain at 10 months post-therapy, but the pathological detection of donor-derived cells in the brain parenchyma suggests the potential of hematopoietic stem cell transplantation for treatment of neurological symptoms in Hunter disease
medicine
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idursulfase treatment appears to be safe and effective in adult Japanese patients with attenuated Mucopolysaccharidosis II
medicine
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measurement of plasma and/or leukocyte IDS activities does not discriminate adequately between mucopolysaccharidosis type II carriers and non-carriers
medicine
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use of enzyme-replacement therapy with recombinant human iduronate-2-sulfatase as a specific treatment for Hunter syndrome. Reductions in liver and spleen volume and in urinary glycoaminoglycan excretion in patients treated with idursulfase. In clinical trials, idursulfase is well tolerated, but in in some patients life-threatening anaphylactic reactions during infusion of idursulfase
medicine
use of zebrafish as a novel tool to better understand lysosomal storage disorder pathogenesis
medicine
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effects of enzyme replacement therapy with iduronate 2-sulfatase on growth in young patients with mucopolysaccharidosis type II. Patients in group 1 received intravenous idursulfase at a standard dose of 0.58 mg/kg weekly for 52-288 weeks. The course of average growth curve for group 1 is very similar to growth pattern in group 2 naive to the enzyme. The average value of body height in subsequent years in group 1 is a little greater than in group 2, however, the difference is not statistically significant. In studied patients with mucopolysaccharidosis type II, idursulfase does not appear to alter the growth patterns
medicine
application of a combined assay for defects in iduronate-2-sulfatase (ID2S) leading to mucopolysaccharidosis II, and N-acetylgalactosamine-6-sulfatase (GALN) and N-acetylgalactosamine-4-sulfatase (ARSB) defects related to mucopolysaccharidosis IVA and MPS VI, respectively. The average enzyme activities of ID2S, GALN, and ARSB in random neonates are 19.6, 1.7, and 13.4 micromol/h/l, respectively. The average enzyme activities of ID2S, GALN, and ARSB in disease-affected individuals are 0.5, 0.3, and 0.3 micromol/h/l, respectively
medicine
structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations identified in patients with mucopolysaccharidosis MPS II. The amino acid substitutions causing MPS II are widely spread over the enzyme molecule and the structural changes of the enzyme protein are generally larger in the severe group than in the attenuated one. The structural changes influence the disease progression
synthesis
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expression and purification of enzyme from Escherichia coli, strategy for improving protein expression and purification
synthesis
expression of protein in Pichia pastoris. The highest production of recombinant IDS is obtained at oxygen-limited conditions using a codon-optimized IDS cDNA.The purified enzyme shows a final activity of 12.45 nmol/mg/h. IDS shows high stability in human serum and is taken up by HEK-293 cells in a dose-dependent manner through mannose receptors
