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4-methylumbelliferyl-alpha-idopyranosiduronic acid 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronate + sulfate
-
-
-
?
4-methylumbelliferyl-alpha-iduronate 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronate + sulfate
4-methylumbelliferyl-alpha-iduronide 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
-
-
-
?
4-methylumbelliferyl-alpha-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
4-methylumbelliferyl-alpha-L-iduronate 2-sulfate + H2O
4-methylumbelliferol + L-iduronate 2-sulfate
4-methylumbelliferyl-alpha-L-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-L-iduronide + sulfate
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
heparan sulfate + H2O
dermatan + sulfate
heparin + H2O
desulfated heparin + sulfate
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol + H2O
O-(alpha-L-idopyranosyluronic acid)-(1-4)-2,5-anhydro-D-mannitol + sulfate
-
-
-
-
?
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol 6-sulfate + H2O
O-(alpha-L-idopyranosyluronic acid)-(1-4)-2,5-anhydro-D-mannitol 6-sulfate + sulfate
-
-
135566, 135567, 135568, 135569, 135570, 135573, 135574, 135575, 135576, 135577, 135578 -
-
?
O-(alpha-L-idopyranosyluronic acid-2-sulfate)-(1-4)-2,5 anhydromannose-6-sulfate
?
-
-
-
?
O-(alpha-L-iduronic acid 2-sulfate)-(1-3)-2,5-anhydro-D-talitol 4-sulfate + H2O
O-(alpha-L-iduronic acid)-(1-3)-2,5-anhydro-D-talitol 4-sulfate + sulfate
-
-
-
-
?
O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid 2-sulfate)-D-O-2,5-anhydro-mannitol 6-sulfate + H2O
O-(alpha-L-iduronic acid)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid)-D-O-2,5-anhydro-mannitol 6-sulfate + sulfate
-
-
-
-
?
O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-O-(beta-D-glucuronic acid or L-iduronic acid)-(1-4)-D-O-(alpha-N-acetylglucosamine)-(1-3)-D-O-gulonic acid + H2O
O-(alpha-L-iduronic acid)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-O-(beta-D-glucuronic acid or L-iduronic acid)-(1-4)-D-O-(alpha-N-acetylglucosamine)-(1-3)-D-O-gulonic acid + sulfate
-
-
-
-
?
O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha glucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid 2-sulfate)-D-O-2,5-anhydro-mannitol 6-sulfate + H2O
O-(alpha-L-iduronic acid)-(1-4)-D-O-(alpha glucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid)-D-O-2,5-anhydro-mannitol 6-sulfate + sulfate
-
-
-
-
?
O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha-N-acetylglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid 2-sulfate)-D-O-2,5-anhydro-mannitol 6-sulfate + H2O
O-(alpha-L-iduronic acid)-(1-4)-D-O (alpha N-acetylglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid)-D-O-2,5-anhydro-mannitol 6-sulfate + sulfate
-
-
-
-
?
additional information
?
-
4-methylumbelliferyl-alpha-iduronate 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronate + sulfate
-
-
-
-
?
4-methylumbelliferyl-alpha-iduronate 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronate + sulfate
-
-
-
?
4-methylumbelliferyl-alpha-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
-
-
-
?
4-methylumbelliferyl-alpha-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
-
-
-
-
?
4-methylumbelliferyl-alpha-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronate 2-sulfate + H2O
4-methylumbelliferol + L-iduronate 2-sulfate
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronate 2-sulfate + H2O
4-methylumbelliferol + L-iduronate 2-sulfate
-
artificial substrate
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
135566, 135567, 135568, 135569, 135570, 135571, 135573, 135574, 135575, 135576, 135577, 135578, 691866 -
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
heparan sulfate + H2O
dermatan + sulfate
-
-
135566, 135567, 135568, 135569, 135570, 135571, 135573, 135574, 135575, 135576, 135577, 135578, 691866 -
-
?
heparan sulfate + H2O
dermatan + sulfate
-
-
-
?
heparan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
heparan sulfate + H2O
dermatan + sulfate
-
-
-
-
?
heparin + H2O
desulfated heparin + sulfate
-
-
135566, 135567, 135568, 135569, 135570, 135571, 135573, 135574, 135575, 135576, 135577, 135578 -
-
?
heparin + H2O
desulfated heparin + sulfate
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the catabolism of the mucopolysaccharides heparan and dermatan sulfate
-
?
additional information
?
-
-
the enzyme is involved in the sequential degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate
-
?
additional information
?
-
-
the enzyme is responsible for heparin sulfate and dermatan sulfate degradation
-
?
additional information
?
-
-
the enzyme is responsible for heparin sulfate and dermatan sulfate degradation
-
?
additional information
?
-
involved in the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate. An enzyme deficiency causes the lysosomal storage disorder muco-polysaccharidosis type II
-
-
?
additional information
?
-
-
involved in the degradation of the glycosaminoglycans heparan sulfate and dermatan sulfate. An enzyme deficiency causes the lysosomal storage disorder muco-polysaccharidosis type II
-
-
?
additional information
?
-
-
mucopolysaccharidosis type II is a lysosomal storage disorder related to a deficiency in the enzyme iduronate-2-sulfatase
-
-
?
additional information
?
-
mechanism follows a SN2 nucleophilic attack of the formylglycine FGH84 on the sulfur atom to generate the covalent formylglycine-S adduct, followed by elimination of bound sulfate and rehydration of the resultant formylglycine aldehyde. Residues H229, H138, D334 and K347 are likely to play active roles in proton transfer or activation of water during the reaction cycle
-
-
?
additional information
?
-
-
mechanism follows a SN2 nucleophilic attack of the formylglycine FGH84 on the sulfur atom to generate the covalent formylglycine-S adduct, followed by elimination of bound sulfate and rehydration of the resultant formylglycine aldehyde. Residues H229, H138, D334 and K347 are likely to play active roles in proton transfer or activation of water during the reaction cycle
-
-
?
additional information
?
-
-
The enzyme has a potential role in normal pathway of lysosomal degradation of secretory peptides and is likely to be essential to maintain pancreatic beta-cell function
-
?
additional information
?
-
-
the enzyme is involved in the catabolism of the mucopolysaccharides heparan and dermatan sulfate
-
?
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A85T
-
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
C84A
-
loss of activity in mutant
C84S
-
artificial mutation in predicted active site. No enzymic acitivity, presence of both the precursor form and processed form of enzyme
D148N
-
mutation identified in patient with mucopolysaccharidosis II
D148V
the mutation perturbs the structure or molecular interactions of the enzyme, leading to loss of enzyme activity and severe phenotype of disease
D269V
-
mutation identified in patient with mucopolysaccharidosis II
D69V
-
mutation identified in patient with mucopolysaccharidosis II
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
G224A
inactive mutant, causing severe phenotype of disease
K227E
the mutation perturbs the structure or molecular interactions of the enzyme, leading to loss of enzyme activity and severe phenotype of disease
L339P
-
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
-
the missense variant has stable mRNA but the residual enzyme activity remains 2.3% of wild type level
Q389X
-
the nonsense mutation leads to premature chain termination at codom 398 and causes mucopolysaccharidosis type II
Q531X
-
mutation identified in patient with mucopolysaccharidosis type II, attenuated phenotype. 2.4% residual activity, presence of a truncated 68000 Da protein form
R101C
the mutant shows 97% of the wild type activity
R443X
the mutation produces truncated protein lacking 20% of the IDS protein, which leads to severe clinical presentations
R468L
-
mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
R468W
-
mutations identified in Taiwanese patients with mucopolysaccharidosis type I, mutations R468Q and R468W together account for 48% of mutations found
R48P
-
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
R88C
-
mutation identified in patient with mucopolysaccharidosis II
R88H
-
13.7% residual enzyme activity in comparison to wild-type enzyme
R88P
-
total absence of residual activity
S333L
-
mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
S349I
-
mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
S369X
-
the nonsense mutation leads to premature chain termination at codom 369 and causes mucopolysaccharidosis type II
W337R
-
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
C84T
-
loss of activity in mutant
C84T
-
artificial mutation in predicted active site. No enzymic acitivity, presence of both the precursor form and processed form of enzyme
P86L
-
mutation identified in patient with mucopolysaccharidosis II
P86L
-
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
R468Q
-
mutation identified in patient with mucopolysaccharidosis type II, severe phenotype. No residual activity, presence of precursor form of enzyme
R468Q
-
mutations identified in Taiwanese patients with mucopolysaccharidosis type I, mutations R468Q and R468W together account for 48% of mutations found
R468Q
the mutant shows 1.4% of the wild type activity
additional information
-
in 25 Hunter syndrome patients 20 mutations of the gene are identified of which 13 mutations are novel
additional information
-
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
-
R88H, R88P, T118I, 959delT, R468Q mutations are identified in Hunter syndrome patients
additional information
-
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
-
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
-
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
-
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
-
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
-
in 25 Hunter syndrome patients 20 mutations of the gene are identified of which 13 mutations are novel
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analysis
direct assay for enzyme activity using substrate 4-methylumbelliferyl alpha-L-idopyranosiduronic acid 2-sulfate and LC-MS/MS based detection
diagnostics
-
sulfatases are potential therapeutic biopharmaceuticals
drug development
-
HIRMAb-IDS fusion protein is a bifunctional IgG-sulfatase fusion protein, specifically engineered for targeted drug delivery across the human blood-brain barrier
additional information
-
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
-
animal model for mucopolysaccharidosis
medicine
-
deficiency in Hunters syndrome, mucopolysaccharidosis II
medicine
-
endocytosis of the recombinant enzyme by human fibroblasts
medicine
-
in humans, the inherited deficiency of the enzyme activity results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
-
in humans, the inherited deficiency of the enzyme activity results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
-
the inherited deficiency results in mucopolysaccharidosis type II
medicine
-
the inherited deficiency results in mucopolysaccharidosis type II, the Hunter syndrome
medicine
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
idursulfase treatment appears to be safe and effective in adult Japanese patients with attenuated Mucopolysaccharidosis II
medicine
-
measurement of plasma and/or leukocyte IDS activities does not discriminate adequately between mucopolysaccharidosis type II carriers and non-carriers
medicine
-
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
-
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
-
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
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Di Natale, P.; Ronsisvalle, L.
Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta
Biochim. Biophys. Acta
661
106-111
1981
Homo sapiens
brenda
Yutaka, T.; Fluharty, A.L.; Stevens, R.L.; Kihara, H.
Purification and some properties of human liver iduronate sulfatase
J. Biochem.
91
433-441
1982
Homo sapiens
brenda
Wasteson, A.; Neufeld, E.F.
Iduronate sulfatase from human plasma
Methods Enzymol.
83
573-578
1982
Homo sapiens
brenda
Archer, I.M.; Harper, P.S.; Wusteman, F.S.
Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids
Biochim. Biophys. Acta
708
134-140
1982
Homo sapiens
brenda
Lissens, W.; Zenati, A.; Liebaers, I.
Polyclonal antibodies against iduronate 2-sulphate sulphatase from human urine
Biochim. Biophys. Acta
801
365-371
1984
Homo sapiens
brenda
Di Natale, P.; Daniele, A.
Iduronate sulfatase from human placenta
Biochim. Biophys. Acta
839
258-261
1985
Homo sapiens
brenda
Constantopoulos, G.; Rees, S.; Cragg, B.G.; Barranger, J.A.; Brady, R.O.
Experimental animal model for mucopolysaccharidosis: suramin-induced glycosaminoglycan and sphingolipid accumulation in the rat
Proc. Natl. Acad. Sci. USA
77
3700-3704
1980
Rattus norvegicus
brenda
Bach, G.; Eisenberg, F., Jr.; Cantz, M.; Neufeld, E.F.
The defect in the Hunter syndrome: deficiency of sulfoiduronate sulfatase
Proc. Natl. Acad. Sci. USA
70
2134-2138
1973
Homo sapiens
brenda
Sjoberg, I.; Fransson, L.A.; Matalon, R.; Dorfman, A.
Hunter's syndrome: a deficiency of L-idurono-sulfate sulfatase
Biochem. Biophys. Res. Commun.
54
1125-1132
1973
Homo sapiens
brenda
Bielicki, J.; Freeman, C.; Clements, P.R.; Hopwood, J.J.
Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties
Biochem. J.
271
75-86
1990
Homo sapiens
brenda
Bielicki, J.; Hopwood, J.J.; Wilson, P.J.; Anson, D.S.
Recombinant human iduronate-2-sulphatase: correction of mucopolysaccharidosis-type II fibroblasts and characterization of the purified enzyme
Biochem. J.
289
241-246
1993
Homo sapiens
brenda
Petruschka, L.; Zschiesche, M.; Bielicki, J.; Seidlitz, G.; Machill, G.; Hopwood, J.J.; Herrmann, F.H.
Mucopolysaccharidosis type II (Hunter syndrome): characterization of the iduronate-2-sulphatase in MPS II skin fibroblasts
J. Inherit. Metab. Dis.
17
89-92
1994
Homo sapiens
brenda
Millat, G.; Froissart, R.; Maire, I.; Bozon, D.
Characterization of iduronate sulphatase mutants affecting N-glycosylation sites and the cysteine-84 residue
Biochem. J.
326
243-247
1997
Homo sapiens
brenda
Coronado-Pons, I.; Novials, A.; Casas, S.; Clark, A.; Gomis, R.
Identification of iduronate-2-sulfatase (IDS) in mouse pancreatic islets
Am. J. Physiol.
10
1-33
2004
Mus musculus
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brenda
Villani, G.R.; Daniele, A.; Balzano, N.; Di Natale, P.
Expression of five iduronate-2-sulfatase site-directed mutations
Biochim. Biophys. Acta
1501
71-80
2000
Homo sapiens
brenda
Bonuccelli, G.; Di Natale, P.; Corsolini, F.; Villani, G.; Regis, S.; Filocamo, M.
The effect of four mutations on the expression of iduronate-2-sulfatase in mucopolysaccharidosis type II
Biochim. Biophys. Acta
1537
233-238
2001
Homo sapiens
brenda
Daniele, A.; Tomanin, R.; Villani, G.R.; Zacchello, F.; Scarpa, M.; Di Natale, P.
Uptake of recombinant iduronate-2-sulfatase into neuronal and glial cells in vitro
Biochim. Biophys. Acta
1588
203-209
2002
Homo sapiens, Rattus norvegicus
brenda
Kim, C.H.; Hwang, H.Z.; Song, S.M.; Paik, K.H.; Kwon, E.K.; Moon, K.B.; Yoon, J.H.; Han, C.K.; Jin, D.K.
Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: identification of 13 novel mutations
Hum. Mutat.
21
449-450
2003
Homo sapiens
brenda
Pan, D.; Jonsson, J.J.; Braun, S.E.; McIvor, R.S.; Whitley, C.B.
"Supercharged Cells" for delivery of recombinant human iduronate-2-sulfatase
Mol. Genet. Metab.
70
170-178
2000
Homo sapiens
brenda
Parkinson, E.J.; Muller, V.; Hopwood, J.J.; Brooks, D.A.
Iduronate-2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients
Mol. Genet. Metab.
81
58-64
2004
Homo sapiens
brenda
Parkinson-Lawrence, E.; Turner, C.; Hopwod, J.; Brooks, D.
Analysis of normal and mutant iduronate-2-sulphatase conformation
Biochem. J.
386
395-400
2005
Homo sapiens (P22304), Homo sapiens
brenda
Dean, C.J.; Bockmann, M.R.; Hopwood, J.J.; Brooks, D.A.; Meikle, P.J.
Detection of mucopolysaccharidosis type II by measurement of iduronate-2-sulfatase in dried blood spots and plasma samples
Clin. Chem.
52
643-649
2006
Homo sapiens
brenda
Bhattacharyya, S.; Tobacman, J.K.
Steroid sulfatase, arylsulfatases A and B, galactose-6-sulfatase, and iduronate sulfatase in mammary cells and effects of sulfated and non-sulfated estrogens on sulfatase activity
J. Steroid Biochem. Mol. Biol.
103
20-34
2007
Homo sapiens
brenda
Lin, S.P.; Chang, J.H.; Lee-Chen, G.J.; Lin, D.S.; Lin, H.Y.; Chuang, C.K.
Detection of Hunter syndrome (mucopolysaccharidosis type II) in Taiwanese: biochemical and linkage studies of the iduronate-2-sulfatase gene defects in MPS II patients and carriers
Clin. Chim. Acta
369
29-34
2006
Homo sapiens
brenda
Chang, J.; Lin, S.; Chuang, C.; Lee-Chen, G.
Characterization of a novel p.S305P and a known c.1006+5G>C splice site mutation in human iduronate-2-sulfatase associated with mucopolysaccharidosis type II
Clin. Chim. Acta
384
167-170
2007
Homo sapiens
brenda
Alves, S.; Mangas, M.; Prata, M.J.; Ribeiro, G.; Lopes, L.; Ribeiro, H.; Pinto-Basto, J.; Lima, M.R.; Lacerda, L.
Molecular characterization of Portuguese patients with mucopolysaccharidosis type II shows evidence that the IDS gene is prone to splicing mutations
J. Inherit. Metab. Dis.
29
743-754
2006
Homo sapiens
brenda
Sukegawa-Hayasaka, K.; Kato, Z.; Nakamura, H.; Tomatsu, S.; Fukao, T.; Kuwata, K.; Orii, T.; Kondo, N.
Effect of Hunter disease (mucopolysaccharidosis type II) mutations on molecular phenotypes of iduronate-2-sulfatase: enzymatic activity, protein processing and structural analysis
J. Inherit. Metab. Dis.
29
755-761
2006
Homo sapiens
brenda
Lualdi, S.; Pittis, M.G.; Regis, S.; Parini, R.; Allegri, A.E.; Furlan, F.; Bembi, B.; Filocamo, M.
Multiple cryptic splice sites can be activated by IDS point mutations generating misspliced transcripts
J. Mol. Med.
84
692-700
2006
Homo sapiens
brenda
Friso, A.; Tomanin, R.; Zanetti, A.; Mennuni, C.; Calvaruso, F.; La Monica, N.; Marin, O.; Zacchello, F.; Scarpa, M.
Gene therapy of Hunter syndrome: evaluation of the efficiency of muscle electro gene transfer for the production and release of recombinant iduronate-2-sulfatase (IDS)
Biochim. Biophys. Acta
1782
574-580
2008
Mus musculus
brenda
Lau, K.C.; Lam, C.W.
Molecular investigations of a novel iduronate-2-sulfatase mutant in a Chinese patient
Clin. Chim. Acta
392
8-10
2008
Homo sapiens
brenda
Keeratichamroen, S.; Ketudat Cairns, J.R.; Wattanasirichaigoon, D.; Wasant, P.; Ngiwsara, L.; Suwannarat, P.; Pangkanon, S.; Kuptanon, J.; Tanpaiboon, P.; Rujirawat, T.; Liammongkolkul, S.; Svasti, J.
Molecular analysis of the iduronate-2-sulfatase gene in Thai patients with Hunter syndrome
J. Inherit. Metab. Dis.
Suppl. 2
303-311
2008
Homo sapiens (P22304), Homo sapiens
brenda
Cordoba-Ruiz, H.; Poutou-Pinales, R.; Echeverri-Pena, O.; Algecira-Enciso, N.; Landazuri, P.; Saenz, H.; Barrera-Avellaneda, L.
Laboratory scale production of the human recombinant iduronate 2-sulfate sulfatase-Like from Pichia pastoris
Afr. J. Biotechnol.
8
1786-1792
2009
Homo sapiens
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brenda
Polito, V.A.; Cosma, M.P.
IDS crossing of the blood-brain barrier corrects CNS defects in MPSII mice
Am. J. Hum. Genet.
85
296-301
2009
Homo sapiens
brenda
Piquer, S.; Casas, S.; Quesada, I.; Nadal, A.; Julia, M.; Novials, A.; Gomis, R.
Role of iduronate-2-sulfatase in glucose-stimulated insulin secretion by activation of exocytosis
Am. J. Physiol. Endocrinol. Metab.
297
E793-E801
2009
Homo sapiens
brenda
Lu, J.Z.; Hui, E.K.; Boado, R.J.; Pardridge, W.M.
Genetic engineering of a bifunctional IgG fusion protein with iduronate-2-sulfatase
Bioconjug. Chem.
21
151-156
2010
Homo sapiens
brenda
Lualdi, S.; Tappino, B.; Di Duca, M.; Dardis, A.; Anderson, C.J.; Biassoni, R.; Thompson, P.W.; Corsolini, F.; Di Rocco, M.; Bembi, B.; Regis, S.; Cooper, D.N.; Filocamo, M.
Enigmatic In Vivo iduronate-2-sulfatase (IDS) mutant transcript correction to wild-type in Hunter syndrome
Hum. Mutat.
31
E1261-E1285
2010
Homo sapiens
brenda
Jones, S.A.; Almassy, Z.; Beck, M.; Burt, K.; Clarke, J.T.; Giugliani, R.; Hendriksz, C.; Kroepfl, T.; Lavery, L.; Lin, S.P.; Malm, G.; Ramaswami, U.; Tincheva, R.; Wraith, J.E.; Wraith, J.E.
Mortality and cause of death in mucopolysaccharidosis type II-a historical review based on data from the Hunter Outcome Survey (HOS)
J. Inherit. Metab. Dis.
32
534-543
2009
Homo sapiens
brenda
Schwartz, I.V.; Pinto, L.L.; Breda, G.; Lima, L.; Ribeiro, M.G.; Mota, J.G.; Acosta, A.X.; Correia, P.; Horovitz, D.D.; Porciuncula, C.G.; Lipinski-Figueiredo, E.; Fett-Conte, A.C.; Sobrinho, R.P.; Norato, D.Y.; Paula, A.C.; Kim, C.A.; Duarte, A.R.; Boy, R.; Leistner-Segal, S.; Burin, M.G.; Giugliani, R.
Clinical and biochemical studies in mucopolysaccharidosis type II carriers
J. Inherit. Metab. Dis.
32
732-738
2009
Homo sapiens
brenda
Moro, E.; Tomanin, R.; Friso, A.; Modena, N.; Tiso, N.; Scarpa, M.; Argenton, F.
A novel functional role of iduronate-2-sulfatase in zebrafish early development
Matrix Biol.
29
43-50
2010
Danio rerio (A0ST40), Danio rerio
brenda
Araya, K.; Sakai, N.; Mohri, I.; Kagitani-Shimono, K.; Okinaga, T.; Hashii, Y.; Ohta, H.; Nakamichi, I.; Aozasa, K.; Taniike, M.; Ozono, K.
Localized donor cells in brain of a Hunter disease patient after cord blood stem cell transplantation
Mol. Genet. Metab.
98
255-263
2009
Homo sapiens
brenda
Okuyama, T.; Tanaka, A.; Suzuki, Y.; Ida, H.; Tanaka, T.; Cox, G.; Eto, Y.; Orii, T.
Japan Elaprase Treatment (JET) study: idursulfase enzyme replacement therapy in adult patients with attenuated Hunter syndrome (Mucopolysaccharidosis II, MPS II)
Mol. Genet. Metab.
99
18-25
2010
Homo sapiens
brenda
Muenzer, J.; Beck, M.; Eng, C.M.; Escolar, M.L.; Giugliani, R.; Guffon, N.H.; Harmatz, P.; Kamin, W.; Kampmann, C.; Koseoglu, S.T.; Link, B.; Martin, R.A.; Molter, D.W.; Munoz Rojas, M.V.; Ogilvie, J.W.; Parini, R.; Ramaswami, U.; Scarpa, M.; Schwartz, I.V.; Wood, R.E.; Wraith, E.
Multidisciplinary management of Hunter syndrome
Pediatrics
124
e1228-e1239
2009
Homo sapiens
brenda
Lu, J.Z.; Boado, R.J.; Hui, E.K.; Zhou, Q.H.; Pardridge, W.M.
Expression in CHO cells and pharmacokinetics and brain uptake in the Rhesus monkey of an IgG-iduronate-2-sulfatase fusion protein
Biotechnol. Bioeng.
108
1954-1964
2011
Homo sapiens
brenda
Sosa, A.C.; Espejo, A.J.; Rodriguez, E.A.; Lizaraso, L.M.; Rojas, A.; Guevara, J.; Echeverri, O.Y.; Barrera, L.A.
Development of a sandwich enzyme linked immunosorbent assay (ELISA) for the quantification of iduronate-2-sulfate sulfatase
J. Immunol. Methods
368
64-70
2011
Homo sapiens
brenda
Morales-Alvarez, E.D.; Rivera-Hoyos, C.M.; Baena-Moncada, A.M.; Landazuri, P.; Poutou-Pinales, R.A.; Saenz-Suarez, H.; Barrera, L.A.; Echeverri-Pena, O.Y.
Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12
J. Microbiol.
51
213-221
2013
Homo sapiens
brenda
Zuber, Z.; RodzynskaSwiatowska, A.; Jurecka, A.; Tylki-Szymanska, A.
The effect of recombinant human iduronate-2-sulfatase (idursulfase) on growth in young patients with mucopolysaccharidosis type II
PLoS ONE
9
e85074
2014
Homo sapiens
brenda
Pimentel, N.; Rodriguez-Lopez, A.; Diaz, S.; Losada, J.C.; Diaz-Rincon, D.J.; Cardona, C.; Espejo-Mojica, A.J.; Ramirez, A.M.; Ruiz, F.; Landazuri, P.; Poutou-Pinales, R.A.; Cordoba-Ruiz, H.A.; Almeciga-Diaz, C.J.; Barrera-Avellaneda, L.A.
Production and characterization of a human lysosomal recombinant iduronate-2-sulfatase produced in Pichia pastoris
Biotechnol. Appl. Biochem.
65
655-664
2018
Homo sapiens (P22304), Homo sapiens
brenda
Lee, K.; Jun, S.H.; Song, S.H.; Park, H.D.; Park, K.U.; Song, J.
Direct assay of iduronate-2-sulfatase for Hunter disease using UPLC-tandem mass spectrometry and fluorogenic substrate
Clin. Biochem.
48
1350-1353
2015
Homo sapiens (P22304)
brenda
Mashima, R.; Ohira, M.; Okuyama, T.; Tatsumi, A.
Quantification of the enzyme activities of iduronate-2-sulfatase, N-acetylgalactosamine-6-sulfatase and N-acetylgalactosamine-4-sulfatase using liquid chromatography-tandem mass spectrometry
Mol. Genet. Metab. Rep.
14
36-40
2018
Homo sapiens (P22304)
brenda
Demydchuk, M.; Hill, C.; Zhou, A.; Bunkoczi, G.; Stein, P.; Marchesan, D.; Deane, J.; Read, R.
Insights into Hunter syndrome from the structure of iduronate-2-sulfatase
Nat. Commun.
8
15786
2017
Homo sapiens (P22304), Homo sapiens
brenda
Saito, S.; Ohno, K.; Okuyama, T.; Sakuraba, H.
Structural basis of mucopolysaccharidosis type II and construction of a database of mutant iduronate 2-sulfatases
PLoS ONE
11
e0163964
2016
Homo sapiens (P22304)
brenda