Information on EC 3.1.6.13 - iduronate-2-sulfatase

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY hide
3.1.6.13
-
RECOMMENDED NAME
GeneOntology No.
iduronate-2-sulfatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycosaminoglycan degradation
-
-
heparin degradation
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
L-iduronate-2-sulfate 2-sulfohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
50936-59-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-iduronate 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronate + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-iduronide 2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-iduronide + sulfate
show the reaction diagram
4-methylumbelliferyl-alpha-L-iduronate 2-sulfate + H2O
4-methylumbelliferol + L-iduronate 2-sulfate
show the reaction diagram
-
artificial substrate
-
-
?
4-methylumbelliferyl-alpha-L-iduronide-2-sulfate + H2O
4-methylumbelliferyl-alpha-L-iduronide + sulfate
show the reaction diagram
-
-
-
-
?
dermatan sulfate + H2O
dermatan + sulfate
show the reaction diagram
heparan sulfate + H2O
dermatan + sulfate
show the reaction diagram
heparin + H2O
desulfated heparin + sulfate
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
O-(alpha-L-idopyranosyluronic acid-2-sulfate)-(1-4)-2,5 anhydromannose-6-sulfate
?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dermatan sulfate + H2O
dermatan + sulfate
show the reaction diagram
heparan sulfate + H2O
dermatan + sulfate
show the reaction diagram
heparin + H2O
desulfated heparin + sulfate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
stimulates at 2 mM
additional information
-
effect of IDS on insulin secretion does not result from increased intracellular Ca2+ signaling
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
-
-
chondroitin 4-sulfate
-
at 0.1 mM
chondroitin 6-sulfate
-
at 0.1 mM
citrate
-
-
Fe3+
-
-
heparan sulfate
-
-
Hg2+
-
-
N-actetylglucosamine 6-sulfate-(1-4)-2,5-anhydro-D-mannitol 6-sulfate
-
competitive inhibitor
-
nitrocatechol sulfate
-
competitive inhibitor
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol
-
competitive inhibitor
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol 6-sulfate
-
competitive inhibitor
O-(alpha-L-idopyranosyluronic acid)-(1-4)-2,5-anhydro-D-mannitol 6-sulfate
-
competitive inhibitor
Phenolphthalein disulfate
-
-
suramin
-
in vivo and in vitro
Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
When islets are cultured in different concentrations of D-glucose, the levels of enzyme mRNA increases, in a dose-dependent manner. Mannoheptulose completely blocks the effect of glucose.
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0192
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol
-
-
0.0025 - 0.043
O-(alpha-L-idopyranosyluronic acid 2-sulfate)-(1-4)-2,5-anhydro-D-mannitol 6-sulfate
0.133 - 0.327
O-(alpha-L-idopyranosyluronic acid-2-sulfate)-(1-4)-2,5 anhydromannose-6-sulfate
0.0007 - 0.0011
O-(alpha-L-iduronic acid 2-sulfate)-(1-3)-2,5-anhydro-D-talitol 4-sulfate
-
pH dependent
0.0014
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
-
pH dependent
0.0019
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
-
pH dependent
0.0025
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
-
pH dependent
0.0031
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
-
pH dependent
0.01 - 0.02
sulfoiduronyl sulfoanhydromannitol
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000006 - 0.00066
-
hrIDS detection by ELISA-sandwich and fluorometric assay in Pichia pastoris culture samples, substrate is 4-methylumbelliferyl-2-iduronate-2-sulfate, pH not specified in the publication, temperature not specified in the publication, overview
0.00063 - 0.0021
-
enzyme determination in human plasma samples by a Fluorometric method, and ELISA double sandwich technique after several freeze and thawing cycles, substrate is 4-methylumbelliferyl-2-iduronate-2-sulfate, pH not specified in the publication, temperature not specified in the publication, overview
0.00083
-
-
0.006
-
untreated neuronal cells, comparison to cells after adenoviral infection
0.00725
-
untreated control cells, comparison to cells after adenoviral infection
11.9
-
-
20.8
-
recombinant protein
78 - 94
-
pH 5.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.9 - 5.7
4.1 - 5.3
-
form C, depending on ionic strength
4.4 - 5.3
-
form B, depending on ionic strength
4.5 - 5.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.03
-
heavy-chain HIRMAb-IDS fusion protein, calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
recombinant enzyme
Manually annotated by BRENDA team
IDS activity already detected at the 64-cell stage, and increases at 6.5 hours post fertilization, during the onset of gastrulation. A gradual decrease of enzymatic activity from 24 hours post fertilization to 5 dpf
Manually annotated by BRENDA team
-
primary epithelial cell, highest activity of galacose 6-sulfatase and aryl sulfatase B of all the cell lines tested
Manually annotated by BRENDA team
-
control
Manually annotated by BRENDA team
embryo and adult
Manually annotated by BRENDA team
embryo
Manually annotated by BRENDA team
-
IDS enzyme activity in mucopolysaccharidosis type II patient at 10 months post-cord blood stem cell transplantation
Manually annotated by BRENDA team
-
IDS enzyme activity in mucopolysaccharidosis type II patient at 10 months post-cord blood stem cell transplantation
Manually annotated by BRENDA team
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
Manually annotated by BRENDA team
vascular mesenchyme of the embryo
Manually annotated by BRENDA team
-
primary myoepithelial cell, highest activity of steryl sulfatase and aryl sulfatase B of all the cell lines tested
Manually annotated by BRENDA team
-
contains only form C; distribution of the forms A, B and C in body fluids
Manually annotated by BRENDA team
-
cultured fibroblasts
Manually annotated by BRENDA team
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000 - 45000
-
SDS-PAGE
42000 - 65000
-
gel filtration
45000
-
Western blot analysis
55000
-
mature form after deglycosylation, recombinant protein, SDS-PAGE
60000
-
after endoglucosidase treatment, SDS-PAGE
76000
-
recombinant IDS, immunoblot analysis
80000 - 100000
-
sucrose density gradient centrifugation
80000 - 115000
-
form A, gel filtration, SDS-PAGE
81000 - 83000
-
form B, gel filtration
83000 - 94000
-
form A, sucrose density gradient centrifugation
90000
-
recombinant protein,SDS-PAGE
108000
-
heavy-chain HIRMAb-IDS fusion protein, calculated from sequence
132000
-
form C, gel filtration
135000
-
heavy-chain HIRMAb-IDS fusion protein, Western blotting
170000 - 190000
-
form B, sucrose density gradient centrifugation
additional information
-
the fusion protein is about 80 kDa larger than the heavy chain of the chimeric HIRMAb
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 42000 + 1 * 18000, SDS-PAGE, reduced
heterotetramer
-
HIRMAb-IDS fusion protein
monomer
-
1 * 80000-90000, sucrose density gradient centrifugation, SDS-PAGE, after treatment with mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
proteolytic maturation of 78000 Da precursor form to 46000-48000 and 55000 Da mature forms
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
-
less stable
135568
7
-
stable at neutral pH
135568
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
30 min, 50% loss of activity of form A, 45 min, 50% loss of activity of form B
64
-
5 min, 50% loss of activity
75
-
2 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
-
in water rapid loss of activity
-
The half-life of intracellular enzyme taken up by peripheral blood lymphocytes from patients with Hunter syndrome from the medium are determined to be 1.9 days.
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, neutral pH, for one year or more
-
4°C, pH 7.2, 150 mM NaCl, several days
-
frozen
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HIRMAb-IDS fusion protein purified by protein A affinity chromatography, to homogeneity
-
of the recombinant protein
-
strategy for improving protein expression and purification of recombinant protein
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AAV type 2/5 vector carrying human IDS cDNA under the control of the cytomegalovirus promoter (AAV2/5CMV-hIDS) administered in day 2 idsy/- mouse pups
-
chimeric IDS-GFP cloned in a pCS2 vector under the control of the cytomegalovirus promoter. The resulting construct transfected into FU20 primary fibroblasts
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
-
expressed in COS-7 cells
-
expressed in islets, alpha and beta clonal cells
-
expression in CHO cell
-
expression in CHO cells
-
expression in COS 7 cells
-
expression in COS cells and lymphoblastoid cells
-
expression in Escherichia coli
-
expression of identified mutations in COS 7 cells
-
full-length IDS cDNA amplified and cloned into the pCR2.1-TOPO vector
-
hIDS c-myc subcloned into pcDNA 3.1/Hygro(-). INS1E cells transiently transfected with the IDS construct
-
HIRMAb-IDS fusion protein (IDS cDNA, encoding Ser26-Pro550, minus the 25 amino acid signal peptide, fused to the carboxyl terminus of the heavy chain of a chimeric monoclonal antibody to the human insulin receptor) expressed in COS cells
-
Pichia pastoris strain GS115:His- transformed with the integrative plasmid pPIC9-hIDS-Like (Clone IDS28)
-
production of the recombinant enzyme by a transfected human clone: Bosc 23 cells and production of the recombinant enzyme by adenoviral transduction of neuronal cells: SK-N-BE
-
production of the recombinant enzyme by adenoviral transduction of glial cells: C6
-
the expression of enzyme from three promoters in four retroviral vectors are studied
-
the recombinant fusion enzyme protein is triaged to the lysosomal compartment of MPS-II fibroblasts, expression in CHO cells as IgG-sulfatase fusion protein with the enzyme fused to a genetically engineered monoclonal antibody against the human insulin receptor, i.e. HIRMAb. The cDNA encoding the human IDS cDNA, minus the sequence encoding the signal peptide, is fused to the carboxyl terminus of the CH3 region of the heavy chain of the chimeric HIRMAb
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
although IDS transcript levels are reduced (51-71% normal) in Hunter syndrome patients, some wild-type IDS protein is detectable
-
IDS expression in the liver and lungs of the control (wild-type and idsy/-) or treated (after 1 month or 18 months of AAV2/5CMV-hIDS therapy) mice
-
IDS expression restrictedly observed in human pancreatic islet
-
IDS is abundantly expressed during early developmental stages, IDS mRNAs is present already at the two-cell stage, pointing to a maternal origin of the transcripts. At later stages, ubiquitous expression from shield to 24 hours post fertilization. At 24 hours post fertilization a visible increased concentration of transcripts detectable in the head, particularly in the region surrounding the midbrain-hindbrain boundary. From the hatching phase (48 hours post fertilization), restriction of IDS transcription to the head, with a more intense staining in the retina, otic vesicles, the tectum and the vascular mesenchyme. More caudally, expression in the liver and pectoral fin buds. At 72 hours post fertilization IDS transcripts mainly present in two distinct areas, corresponding to the splanchnocranium and the gut, and a faint staining still in the otic vesicle. This expression pattern becomes more defined at 120 hours post fertilization, when the intensity of the hybridization signal in the gut and splanchnocranium. In the adult stage, IDS mRNAs in all the examined tissues
IDS-Like expression is induced by methanol addition
-
knocking down with antisense morpholino oligos, significant decrease in the enzymatic activity after 24 hours post-morpholino injection in morphants (72.3% of the control). Inability of the morpholino to completely suppress the IDS activity due to maternally derived enzyme. Increased transforming growth factor beta signalling is tightly associated with downregulation of iduronate sulfatase function
no IDS expression in the brain samples of the control (wild-type and idsy/-) or treated (after 1 month or 18 months of AAV2/5CMV-hIDS therapy) mice
-
presence of wild-type IDS mRNA-transcripts in Hunter syndrome patients, but no wild-type IDS genomic sequence detectable
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
medicine
synthesis
-
expression and purification of enzyme from Escherichia coli, strategy for improving protein expression and purification
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