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
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x-linked
- dermatan
- heparan
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multisystemic
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sulfatases
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hepatosplenomegaly
- medicine
- arylsulfatase
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mpsii
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x-chromosome
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enzyme-replacement
- analysis
- synthesis
- alpha-l-iduronidase
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neuronopathic
-
infusion-related
- drug development
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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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General Information on EC 3.1.6.13 - iduronate-2-sulfatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
physiological function
additional information
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development of an expression system for human recombinant IDS in Pichia pastoris and of a detection method for enzyme detection during production and purification processes, which can be used also to measure the enzyme in human fluids, immunoquantification assay using rabbit IgG and chicken IgY, overview
malfunction
downregulation of IDS may be responsible for severe early developmental defects, including a misshapen trunk and abnormal craniofacial cartilages, which is mediated by depauperation of sox10-expressing neural crest cell precursors, which is reverted through the administration of the recombinant enzyme
malfunction
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Hunter syndrome is caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase. In the absence of sufficient enzyme activity, glycosaminoglycans accumulate in the lysosomes. Complete deletions of the I2S gene (IDS) always result in a severe phenotype, as do complex rearrangements of IDS. Several missense mutations are associated with a severe phenotype (p.R468Q,89-94 p.R468W,95-99 and p.S333L96,100), although each one has in patients with an intermediate or attenuated phenotypes. The mutation c.1122C3T (which creates an alternate splice site with the loss of 20 amino acids) is primarily associated with the attenuated phenotype
malfunction
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Italian Hunter syndrome patients show a lack of concordance between IDS genomic DNA and cDNA: presence of wild-type IDS sequence as well as the mutated sequence in cDNA from one or more tissues, but no wild-type IDS sequence is evident in the genomic DNAs derived from these patients, a correction mechanism such as RNA editing may potentially account for this. These Hunter syndrome patients are hemizygous respectively for a nonsense mutation (c.22C>T,p.R8X) and a frameshift micro-insertion (c.10insT,p.P4Sfs) in their genomic DNA. Since both p.R8X mutations are inherited from carrier mothers, somatic mosaicism can be excluded
malfunction
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iduronate-2-sulfate sulfatase, IDS, deficiency causes the Hunter syndrome ormucopolysaccharidosis type II
malfunction
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mucopolysaccharidosis, MPS, type II is caused by mutations in the lysosomal enzyme, iduronate-2-sulfatase. MPS-II affects the brain and enzyme replacement therapy is ineffective for the brain, because the enzyme does not cross the blood-brain barrier
physiological function
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a 6-year-old male suffering from a severe type of Hunter disease (deficiency of IDS) with cord blood stem cell transplantation died at 10 months post-therapy due to a laryngeal post-transplantation lymphoproliferative disorder
physiological function
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a deficiency of iduronate-2-sulfatase causes mucopolysaccharidosis type II (Hunter syndrome), which is a progressive, multisystemic disease: patients with the severe form of the disease have cognitive impairment and typically die in the second decade of life, whereas patients with the less severe form do not experience significant cognitive involvement and may survive until the fifth or sixth decade of life
physiological function
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HIRMAb-IDS fusion protein crosses the blood-brain barrier on the endogenous insulin receptor and acts as a molecular Trojan horse to ferry the IDS into brain. The fusion protein is taken up by Hunter fibroblasts, and the accumulation of glycosoaminoglycans in fibroblasts null for the sulfatase is decreased 84% by treatment with the fusion protein. The fusion protein heavy chain reacts with antibodies to both human IgG and human IDS. The fusion protein is a bifunctional molecule and binds both the HIR extracellular domain with comparable affinity to the chimeric HIRMAb and has high IDS enzyme activity
physiological function
iduronate sulfatase plays a critical role during early vertebrate developments
physiological function
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in AAV2/5CMV-hIDS-injected mucopolysaccharidosis type II mice with Hunter syndrome, rescue of brain defects. The central nervous system correction arises from the crossing of the blood-brain barrier by the IDS enzyme
physiological function
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male patients, ages 21-53 years, receiving weekly intravenous infusions of 0.5 mg/kg idursulfase for 12 months, show significant reductions in lysosomal storage and several clinical improvements. Idursulfase is generally well-tolerated. Infusion-related reactions occur in 50% of patients and are mostly mild with transient skin reactions that do not require medical intervention. Two infusion-related reactions are assessed as serious (urticaria and vasovagal syncope)
physiological function
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mucopolysaccharidosis type II carriers show lower plasma and leukocyte IDS activities but this reduction is generally associated neither with age, changes in levels of urinary glycosaminoglycans nor with the occurrence of clinical manifestations
physiological function
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overexpression of IDS enhances glucose-induced insulin secretion in INS1E cells by activation of the exocytotic process. IDS overexpression is associated with a gain of function detected by a reduction in heparan sulfate content. IDS potentiates the glucose-stimulated insulin secretory response compared with controls (61%) with no changes in insulin mRNA levels or insulin peptide content. Increase in the number of granules in the immediate vicinity of the plasma membrane in IDS-transfected cells and a decrease in total vesicles per square micrometer. IDS overexpression induces phosphorylation of protein kinase C alpha and its newly myristoylated alanine-rich C kinase substrate, MARCKS
physiological function
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recombinant IDS-Like activity increases when passed from culture M6 (11.34 g/l of glycerol) to M7 (25.53 g/l of glycerol), from 14.7 to 29.5 nmol/h/mg of total protein, between the 33 and 47 h of culture. In M8 (40.13 g/l of glycerol), the recombinant IDS-Like activity is 7.3 nmol/h/mg of total protein at 47h of culture. In M9 (83.32 g/l of glycerol), no recombinant IDS-Like activity is detected. Recombinant IDS-Like activity is lower when extra-cellular proteolytic activity increases
