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Information on EC 3.2.1.76 - L-iduronidase
for references in articles please use BRENDA:EC3.2.1.76
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.76 L-iduronidase
The enzyme appears in viruses and cellular organisms
- 3.2.1.76
- mucopolysaccharidosis
- lysosomal
- hurler
- glycosaminoglycans
-
scheie
- dermatan
- heparan
-
hurler-scheie
-
hematopoietic
- corneal
- medicine
-
mucopolysaccharide
-
intrathecal
-
clouding
-
hepatosplenomegaly
-
iduronate
- pompe
- pharmacology
-
enzyme-replacement
-
4-methylumbelliferyl
-
facies
-
mckusick
- diagnostics
-
dysostosis
- fabry
- drug development
- gaucher
Reaction Schemes
showSynonyms
alpha-l-iduronidase, laronidase, iduronidase, alpha-iduronidase, l-iduronidase, alpha-l-iduronidase a, hidua, aldurazyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aldurazyme
alpha-L-iduronidase
hIDUA
IDU
IDUA
additional information
the enzyme belongs to the CAZY 39 structural family
alpha-L-iduronidase
-
-
-
-
alpha-L-iduronidase
-
-
alpha-L-iduronidase
-
IDUA
-
-
IDUA
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate
-
-
-
-
hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate
active site structure, active site residues, overview
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glycosaminoglycan alpha-L-iduronohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9073-56-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-anhydro-3-O-alpha-L-idopyranuronosyl-D-mannitol + H2O
?
-
Substrates: -
Products: -
Products: -
?
2,5-anhydro-4-O-alpha-L-idopyranuronosyl-D-mannitol 6-sulfate + H2O
?
-
Substrates: -
Products: -
Products: -
?
4-methylcoumarin-7-yl-alpha-L-iduronic acid + H2O
4-methylcoumarin + alpha-L-iduronic acid
-
Substrates: design and development of an improved and less expensive synthesis method for the fluorogenic substrate, overview. The method is based on the double ketal fixation of the 1,2 and 3,5-hydroxy groups of D-glucose to form a cis-anti-cis-fused tricyclic D-glucofuranosyl derivative, which could undergo elimination to form a 5-exo-double bond followed by electrophilic addition, a Mitsunobu-type glycosylation reaction is used for the coupling of the hemiacetal with the acceptor
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
4-methylumbelliferyl-alpha-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
4-methylumbelliferyl-alpha-L-iduronide + methanol
?
-
Substrates: methanolysis
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronoside + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-idopyranosiduronate + H2O
4-nitrophenol + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-iduronide + H2O
4-nitrophenol + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
5-fluoro-alpha-L-idopyranosyluronic acid fluoride + H2O
fluoride + ?
-
Substrates: -
Products: -
Products: -
?
alpha-L-iduronosyl(1-4)anhydromannitol-6-sulfate + H2O
?
Substrates: -
Products: -
Products: -
?
alpha-L-iduronosyl-(1->3)-2,5-anhydro-D-talitol 4-sulfate + H2O
?
-
Substrates: -
Products: -
Products: -
?
alpha-L-iduronysyl-(alpha-1,4)2,5-anhydro-D-mannitol-6-sulfate + H2O
2,5-anhydro-D-mannitol 6-sulfate + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
dermatan sulfate + H2O
? + alpha-iduronic acid
Substrates: -
Products: -
Products: -
?
glycosaminoglycan + H2O
? + alpha-iduronic acid
Substrates: -
Products: -
Products: -
?
heparan sulfate + H2O
? + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
IdoA-GlcNAc6S-IdoA2S-anM6S + H2O
?
-
Substrates: O-(alpha-L-iduronic acid)-(1,4)-D-O-(alpha-N-acetylglucosamine 6-sulphate)-L-O-(alpha-iduronic acid 2-sulphate)-O-D-2,5-anhydro-D-mannitol 6-sulphate
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
-
Substrates: -
Products: -
Products: -
?
phenyl alpha-L-iduronide + H2O
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves alpha-L-iduronic acid from the nonreducing ends of dermatan sulfate, heparin, and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the sequential degradation of heparan sufate and dermatan sulfate, enzyme deficiency results in the accumulation and urinary secretion of partially degraded glycosaminoglycans and causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of recombinant enzyme with and without a C-terminal ER-retention signal from seeds of Brassica napus and Nicotiana tabacum, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves terminal alpha-iduronic acid residues from glycosaminoglycan, heparan sulfate and dermatan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes terminal iduronic acid residues on glycosaminoglycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyses the glycosidic bond between the terminal L-iduronic acid and the second sugar of N-acetylgalactosamine-4-sulfate/N-sulfo-D-glucosamine-6-sulfate, which are the major components of dermatan/heparan sulfate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-anhydro-3-O-alpha-L-idopyranuronosyl-D-mannitol + H2O
?
-
Substrates: -
Products: -
Products: -
?
2,5-anhydro-4-O-alpha-L-idopyranuronosyl-D-mannitol 6-sulfate + H2O
?
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
alpha-L-iduronosyl-(1->3)-2,5-anhydro-D-talitol 4-sulfate + H2O
?
-
Substrates: -
Products: -
Products: -
?
dermatan sulfate + H2O
? + alpha-iduronic acid
Substrates: -
Products: -
Products: -
?
glycosaminoglycan + H2O
? + alpha-iduronic acid
Substrates: -
Products: -
Products: -
?
heparan sulfate + H2O
? + alpha-L-iduronic acid
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves alpha-L-iduronic acid from the nonreducing ends of dermatan sulfate, heparin, and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in mucopolysaccharidosis type I
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the sequential degradation of heparan sufate and dermatan sulfate, enzyme deficiency results in the accumulation and urinary secretion of partially degraded glycosaminoglycans and causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes mucopolysaccharidosis type I, MPSI
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves terminal alpha-iduronic acid residues from glycosaminoglycan, heparan sulfate and dermatan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes terminal iduronic acid residues on glycosaminoglycans
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyses the glycosidic bond between the terminal L-iduronic acid and the second sugar of N-acetylgalactosamine-4-sulfate/N-sulfo-D-glucosamine-6-sulfate, which are the major components of dermatan/heparan sulfate
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3R,4S,5S,6R)-3,4,5-trihydroxy-7-[8-[4-([[6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanoyl]amino]methyl)-1H-1,2,3-triazol-1-yl]octyl]-7-azabicyclo[4.1.0]heptane-2-carboxylic acid
-
(1R,2R,3R,4S,5S,6R)-7-(8-azidooctyl)-3,4,5-trihydroxy-7-azabicyclo[4.1.0]heptane-2-carboxylic acid
irreversible inhibitor
(1R,2S,3S,4R,5S,6R)-7-(8-azidooctyl)-5-(hydroxymethyl)-7-azabicyclo[4.1.0]heptane-2,3,4-triol
-
(2R,3R,4R,5S,6S)-3,4,5-trihydroxy-6-(2-(2-(2-(phosphonooxy)phenyl)acetamido)ethyl)piperidine-2-carboxylic acid
0.25 mM, 43% inhibition
-
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(2-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
-
-
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(3-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
-
-
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(4-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
-
-
(2R,3S,4R,5R,6S)-6-(2-aminoethyl)-3,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid
-
-
(5R,6R,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
-
(5R,6S,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
-
(5S,6R,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
-
2-fluoro-alpha-L-idopyranosyluronic acid fluoride
-
reversible, competitive with 4-nitrophenyl-alpha-L-idopyranosiduronate, activity drops down immediately after inhibitor is added
2-[(1E,3E,5E)-5-[1-(6-[[(1-[8-[(1R,2R,3R,4S,5S,6R)-2-carboxy-3,4,5-trihydroxy-7-azabicyclo[4.1.0]heptan-7-yl]octyl]-1H-1,2,3-triazol-4-yl)methyl]amino]-6-oxohexyl)-3,3-dimethyl-1,3-dihydro-2H-indol-2-ylidene]penta-1,3-dien-1-yl]-1,3,3-trimethyl-3H-indol-1-ium
irreversible inhibitor
5-fluoro-alpha-L-idopyranosyluronic acid fluoride
-
reversible, competitive with 4-methylumbelliferyl-alpha-L-iduronide, activity drops down immediately after inhibitor is added
EDTA
-
competitive, equal inhibition of enzyme from healthy individuals and mucopolysaccharidosis type I patients
[(2S,3R,4R)-3,4-dihydroxy-5-oxotetrahydrofuran-2-yl](hydroxy)acetic acid
-
competitive inhibitor
CuCl2
-
strong noncompetitive inhibitor for enzyme from healthy individuals and mucopolysaccharidosis type I patients
NaCl
-
healthy individuals and 40% of heterocygotic mucopolysaccharidosis type I patients, activating for 60% of heterocygotic mucopolysaccharidosis type I patients
additional information
-
not inhibited by 6-sodium 5-amino-5-deoxy-D-glucarate-1,5-lactam, 6-sodium 5-amino-5-deoxy-D-galactarate-1,5-lactam, 6-sodium 5-amino-5-deoxy-L-altrarate-1,5-lactam, and 4-amino-4,5-dideoxy-L-arabinaro-1,4-lactam
-
additional information
-
uptake of laronidase by F17 and F592 cells is strongly inhibited in the presence of 5.0 mmol/l mannose 6-phosphate in the culture medium. Uptake of the enzyme by MC3T3-E1 cells is strongly inhibited by the addition of 5.0 mmol/l M6P to the culture medium, but moderately inhibited by the addition of 5.0 mmol/l Man, as in the case of F665 cells
-
additional information
-
deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the synthesis of the CnABI3 (ABscisic acid Insensitive3) protein is able to transactivate the IDUA gene expression driven by the arcelin promoter, particularly in the presence of 0.15-0.2 mM (S)-(+)-abscisic acid
-
additional information
-
the synthesis of the CnABI3 (ABscisic acid Insensitive3) protein is able to transactivate the IDUA gene expression driven by the arcelin promoter, particularly in the presence of 0.15-0.2 mM (S)-(+)-abscisic acid
-
additional information
-
intracellular IDUA activity increases dose-dependently in both MC3T3-E1 and F665 cells. When laronidase is added to the medium at a low concentration (0.10 mg/ml) there is no difference in the uptake between them. Increase in the enzyme activity is always lower in MC3T3-E1 cells than in F665 ones when laronidase is added to the medium at the concentration of 1.0m g/ml or more, thus uptake of laronidase is lower in MC3T3-E1 cells than in F665 cells
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
4-methylumbelliferyl alpha-L-iduronide
pH 4.2, 32°C, recombinant wild-type enzyme
0.12
4-methylumbelliferyl alpha-L-iduronide
recombinant enzyme, at pH 3.5 and 37°C
0.13
4-methylumbelliferyl alpha-L-iduronide
Aldurazyme, at pH 3.5 and 37°C
0.21
4-methylumbelliferyl-alpha-L-iduronide
-
pH 2.8, 37°C, enzyme from healthy individuals in the presence of 10 mM CuCl2l
0.22
4-methylumbelliferyl-alpha-L-iduronide
-
pH 2.8, 37°C, enzyme from healthy individuals
0.38
4-methylumbelliferyl-alpha-L-iduronide
-
37°C, enzyme from mucopolysaccharidosis patients group II
0.48
4-methylumbelliferyl-alpha-L-iduronide
-
pH 2.8, 37°C, enzyme from healthy individuals in the presence of 20 mM EDTA
0.49
4-methylumbelliferyl-alpha-L-iduronide
-
37°C, enzyme from mucopolysaccharidosis patients group I
0.6
4-methylumbelliferyl-alpha-L-iduronide
-
37°C, enzyme from healthy individuals
0.81
4-methylumbelliferyl-alpha-L-iduronide
-
pH 2.8, 37°C, enzyme from healthy individuals in the presence of 0.1 M NaCl
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.4
4-methylumbelliferyl alpha-L-iduronide
Aldurazyme, at pH 3.5 and 37°C
11.8
4-methylumbelliferyl alpha-L-iduronide
recombinant enzyme, at pH 3.5 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
(2R,3S,4R,5R,6S)-6-(2-aminoethyl)-3,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid
pH and temperature not specified in the publication
-
5
(5R,6R,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
Ki above 5 mM, at pH 4.5 and 37°C
5
(5R,6S,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
Ki above 5 mM, at pH 4.5 and 37°C
1.3
(5S,6R,7S,8S)-5,6,7,8-tetrahydro-6,7,8-trihydroxytetrazolo[1,2-a]pyridine-5-carboxylate
-
at pH 4.5 and 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0651
(1R,2R,3R,4S,5S,6R)-3,4,5-trihydroxy-7-[8-[4-([[6-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)hexanoyl]amino]methyl)-1H-1,2,3-triazol-1-yl]octyl]-7-azabicyclo[4.1.0]heptane-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0406
(1R,2R,3R,4S,5S,6R)-7-(8-azidooctyl)-3,4,5-trihydroxy-7-azabicyclo[4.1.0]heptane-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0122
(1R,2S,3S,4R,5S,6R)-7-(8-azidooctyl)-5-(hydroxymethyl)-7-azabicyclo[4.1.0]heptane-2,3,4-triol
Homo sapiens
pH and temperature not specified in the publication
0.001
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(2-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.004
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(3-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.0054
(2R,3S,4R,5R,6S)-3,4,5-trihydroxy-6-(2-(2-(4-(phosphonooxy)phenyl)acetamido)ethyl)tetrahydro-2H-pyran-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.0067
(2R,3S,4R,5R,6S)-6-(2-aminoethyl)-3,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.0581
2-[(1E,3E,5E)-5-[1-(6-[[(1-[8-[(1R,2R,3R,4S,5S,6R)-2-carboxy-3,4,5-trihydroxy-7-azabicyclo[4.1.0]heptan-7-yl]octyl]-1H-1,2,3-triazol-4-yl)methyl]amino]-6-oxohexyl)-3,3-dimethyl-1,3-dihydro-2H-indol-2-ylidene]penta-1,3-dien-1-yl]-1,3,3-trimethyl-3H-indol-1-ium
Homo sapiens
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000014 - 0.000027
mucopolysaccharidosis type I mutant enzymes, immunocapture-enriched from skin fibroblast
0.000005 - 0.00011
-
activity levels from the same specimens of heterozygous mice vary greatly with different substrate concentrations of 4-methylumbelliferyl-alpha-L-iduronide, comparison of activities in livers at 15 different concentrations, overview. pH and temperature not specified in the publication
0.00003 - 0.000093
wild-type enzyme, immunocapture-enriched from skin fibroblast
0.0029
-
recombinant enzyme, using 4-methylumbelliferyl-alpha-L-iduronide as a substrate
0.0033 - 0.0053
-
wild-type cell lines, pH not specified in the publication, 37°C
0.018
-
native enzyme, using 4-methylumbelliferyl-alpha-L-iduronide as a substrate
0.03
-
recombinant enzyme, using 4-methylumbelliferyl-alpha-L-iduronide as a substrate
additional information
-
specific activity in healthy individuals was found to be higher than specific activity in mucopolysaccharidosis patients group I but similar with mucopolysaccharidosis patients group II
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 3.5
4.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
171551, 171553, 171554, 171555, 171556, 171558, 171559, 171560, 171561, 171562, 171563, 171564, 171566, 171568, 171569, 171570, 171571, 654043, 654383, 654716, 654856, 655246, 655683, 663579
-
-
brenda
-
666375, 680058, 680077, 681942, 681947, 682247, 682312, 696554, 697827, 699314, 699732, 700229, 700582, 709198, 709388, 709963, 709972, 710324, 715115, 716239
-
-
brenda
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
from healthy humans and mucopolysaccharidosis type I patients
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
with transfected CHO-K1 cells less than 10% of enzyme is found to be secreted into the medium
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the enzyme is involved in the stepwise degradation of glycosaminoglycans
physiological function
-
the enzyme is involved in the degradation of the glycosaminoglycans dermatan sulfate and heparan sulfate
additional information
-
the enzyme uses its own N-glycan as a substrate binding and catalytic module. The mannose residue of the N-glycan attached to N372 constitutes a part of the substrate-binding pocket and interacts directly with a substrate. The kinetics of native and deglycosylated hIDUA suggest that the N-glycan is also involved in catalytic processes. Concanavalin A pull-down assay shows that PNGase F-resistant N-glycans are essential for the enzyme activity. Enzyme and substrate binding site structures and enzyme-substrate interaction analysis, overview
malfunction
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder with features ranging over a continuum from mild to severe which is inherited in an autosomal recessive manner
malfunction
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder
malfunction
-
mucopolysaccharidosis type I arises from a deficiency in the alpha-L-iduronidase enzyme
malfunction
-
mucopolysaccharidosis type I is caused by a deficiency in lysosomal alpha-L-iduronidase activity
malfunction
-
mucopolysaccharidosis type I is caused by a deficiency in lysosomal alpha-L-iduronidase activity
malfunction
enzyme deficiency causes mucopolysaccharidosis type I, patients with MPS I developmental retardation, gross facial features, an enlarged and deformed skull, a small stature, corneal opacities, hepatosplenomegaly, valvular heart defects, thick skin, joint contractures and hernias
malfunction
-
deficiency of the enzyme leads to progressive accumulation of glycosaminoglycans, dermatan and heparan sulfate, in all organs and tissues, mucopolysccharidosis I is a lysosomal storage disorder that results from deficiency in the lysosomal enzyme alpha-L-iduronidase. Infusions of intravenous enzyme improves hepatosplenomegaly, pulmonary function, ambulation, jointmobility, cardiac function, and cognitive and neuroradiological progress
malfunction
-
mucopolysaccharidosis type I, MPS I, is an autosomal recessively inherited lysosomal storage disorder caused by the lack of alpha-L-iduronidase which leads to accumulation of glycosaminoglycans in the lysosome, genotyping of cell lines with residual enzyme activity, overview
malfunction
-
enzyme dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I. The defect of the enzyme leads to excess storage of dermatan/heparan sulfate and causes a systemic disorder, MPS I, involving progressive mental retardation, gross facial features, an enlarged and deformed skull, a small stature, corneal opacities, hepatosplenomegaly, valvular heart defects, thick skin, joint contractures, and hernias
malfunction
-
mucopolysaccharidosis I is an autosomal recessive lysosomal storage disease due to deficient alpha-L-iduronidase activity. It results in the accumulation of the glycosaminoglycans heparan and dermatan sulfate and leads to several clinical manifestations
malfunction
mucopolysaccharidosis type I is caused by the deficient activity of the enzyme
malfunction
Mucopolysaccharidosis type I Hurler syndrome (MPS IH) is a severe lysosomal storage disorder caused by alpha-L-iduronidase (IDUA) deficiency. Premature truncation mutations (PTC) are the most common (50%-70%) type of IDUA mutations and correlate with MPS IH. Nonsense suppression therapy is a therapeutic approach that aims to induce stop codon readthrough. The effect on stop codon readthrough is determined by changes in protein production and enzymatic activities of COS-7 cells expressing mutant transcripts
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0D9RSH1_CHLSB
653
0
72963
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1U7QR52_MESAU
643
0
72479
TrEMBL
other Location (Reliability: 1)
A0A2J8K710_PANTR
660
0
73546
TrEMBL
Mitochondrion (Reliability: 1)
A0A2K5KN88_CERAT
653
0
72870
TrEMBL
other Location (Reliability: 3)
A0A2K5PC52_CEBIM
653
0
72676
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2K6CPR0_MACNE
653
0
72882
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2Y9G2M1_NEOSC
643
0
71639
TrEMBL
other Location (Reliability: 2)
A0A673UBZ2_SURSU
639
0
71528
TrEMBL
other Location (Reliability: 2)
A0A6J1ZPF0_ACIJB
643
0
71729
TrEMBL
Mitochondrion (Reliability: 2)
A0A7J8JW87_MOLMO
602
0
67236
TrEMBL
other Location (Reliability: 2)
A0A8B7W6M3_CASCN
654
0
73167
TrEMBL
Mitochondrion (Reliability: 3)
A0A8C5V0A1_MICMU
578
0
63822
TrEMBL
other Location (Reliability: 2)
A0A8C8U8W2_PERMB
643
0
72471
TrEMBL
-
A0A8C8U0U6_PERMB
596
0
67158
TrEMBL
-
A0A8C8WRT4_PANLE
650
0
72293
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D2IRI3_UROPR
639
0
71329
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8U0NA36_MUSPF
643
0
72052
TrEMBL
Secretory Pathway (Reliability: 2)
A0A9J7GE11_CRIGR
648
0
73045
TrEMBL
Chloroplast (Reliability: 5)
A0AAU9ZW41_PHORO
643
0
72196
TrEMBL
Secretory Pathway (Reliability: 1)
A0ABD2EL71_DAUMA
600
0
66682
TrEMBL
other Location (Reliability: 1)
E1BDR2_BOVIN
651
0
72382
TrEMBL
Secretory Pathway (Reliability: 1)
H0XDM7_OTOGA
639
0
71044
TrEMBL
Secretory Pathway (Reliability: 1)
H2QP30_PANTR
653
0
72738
TrEMBL
other Location (Reliability: 4)
I3M8U1_ICTTR
592
0
66195
TrEMBL
other Location (Reliability: 4)
Q6PEP9_MOUSE
643
0
72185
TrEMBL
Secretory Pathway (Reliability: 1)
Q8BLF6_MOUSE
596
0
66931
TrEMBL
other Location (Reliability: 2)
U3CT60_CALJA
653
0
72693
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
x * 83000, recombinant wild-type enzyme, SDS-PAGE, x * 125000, recombinant RAP-fusion enzyme, SDS-PAGE
49000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
60000
65000
69000
74000
76600
-
x * 76600, recombinant glycosylated enzyme expressed from Brassica napus seeds, SDS-PAGE, x * 76700, recombinant glycosylated enzyme expressed from Nicotiana tabacum seeds, SDS-PAGE
76700
-
x * 76600, recombinant glycosylated enzyme expressed from Brassica napus seeds, SDS-PAGE, x * 76700, recombinant glycosylated enzyme expressed from Nicotiana tabacum seeds, SDS-PAGE
77000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
83000
85000
65000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
69000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
74000
-
wild type enzyme, SDS-PAGE, intracellulary processed to form fragments of 69000 Da and 65000 Da
74000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
83000
-
x * 83000, recombinant wild-type enzyme, SDS-PAGE, x * 125000, recombinant RAP-fusion enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
?
-
x * 83000, recombinant wild-type enzyme, SDS-PAGE, x * 125000, recombinant RAP-fusion enzyme, SDS-PAGE
?
-
x * 76600, recombinant glycosylated enzyme expressed from Brassica napus seeds, SDS-PAGE, x * 76700, recombinant glycosylated enzyme expressed from Nicotiana tabacum seeds, SDS-PAGE
additional information
structure determination, PDB code 1Y24, using the crystal structure of the beta-xylosidase from Thermoanaerobacterium saccharolyticum, EC 3.2.1.37, structure modeling
additional information
-
structure determination, PDB code 1Y24, using the crystal structure of the beta-xylosidase from Thermoanaerobacterium saccharolyticum, EC 3.2.1.37, structure modeling
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
glycoprotein
-
oligomannose 7-bisphosphate is bound to the enzyme, with a much higher amount on the recombinant wild-type enzyme compared to the recombinant RAP fusion enzyme
glycoprotein
-
the enzyme is N-glycosylated. The carboxy-terminal endoplasmic reticulum-retention motif, SEKDEL, influences the N-linked glycosylation of the recombinant enzyme
glycoprotein
-
N-glycosylation, deglycoslyation b peptide N-glycosidase F from Flavobacterium meningosepticum and neuraminidase from Clostridium perfringens. The N-glycan pools consists of oligomannosidic glycans (mainly Man7, Man8, Man9 as well as Man9 + Glc), complex type glycans with up to three antennae. Sialylation as well as fucosylation are observed on almost all complex type glycans
glycoprotein
-
N-glycosylation at N110, N190, N336, N372, N415, and N451 in subunit A, and at N110, N190, N336, N372, N415, and N451 in subunit B, glycan structures, overview. The enzyme uses its own N-glycan as a substrate binding and catalytic module. The mannose residue of the N-glycan attached to N372 constitutes a part of the substrate-binding pocket and interacts directly with a substrate. The kinetics of native and deglycosylated hIDUA suggest that the N-glycan is also involved in catalytic processes. Deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity. Concanavalin A pull-down assay shows that PNGase F-resistant N-glycans are essential for the enzyme activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from different solution using the hanging-drop crystallization method
-
purified recombinant enzyme, hanging drop vapour diffusion method, 4 mg/ml protein, mixing of 0.008 ml of both protein solution and reservoir solution, the latter containing 18% w/v PEG 3350, 0.18 M K/Na-tartrate, 3% w/v PEG MME 5000, 0.02 M ammonium sulfate, and 0.01 M MES-Na, pH 6.5, 25°C, 2-3 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, mercury-derivative crystals by single-wavelength anomalous dispersion data, Hg peak wavelength
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A327P
A79V
D315Y
E182K
E276K
-
E276K/E276K is a naturally occuring rare homozygous mutant genotype with only residual enzyme activity and thermal instability at 37°C
F602I
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 5fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
G265R
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows reduced activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
H82Q
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows 8fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
I270S/P533R/R268X
-
identification of naturally occurring mutation of a tunesian patient, homoallelic for P533R mutation, heteroallelic for missense mutation I270S and nonsense mutation R268X, and a deletion mutation in exon 13, the mutations are involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, the patient shows the Huler phenotype, overview
L218P
L238Q
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 3.5fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
L346R
L490P
M1T
the mutation is identified in a Chinese family with autosomal recessive mucopolysaccharidosis I
P533R
Q380R
Q70X
R363C
R363H
-
the missense mutation is associated with hepatosplenomegaly, joint stiffness, corneal clouding, and slightly mental delay in mucopolysaccharidosis type I patients and displays 2.3% of wild type activity
R383H
R89Q
S423R
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows 11fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
T364M
W402X
additional information
A327P
-
A327P/A327P and A327P/unknown, naturally occuring homozygous and indefinite mutant genotypes with only residual enzyme activity at 37°C
A79V
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 2fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
E182K
-
mutation found in patients with mucopolysaccharidosis type I, catalytically inactive
P533R
-
identification of naturally occurring mutation of two tunesian patient, homoallelic for P533R mutation, the mutation is involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, the patient shows the Huler-Scheie phenotype, overview
R363C
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, inactive recombinant mutant
additional information
identification and molecular characterization of 14 different enzyme mutations and 13 different polymorphic changes present in 10 mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
additional information
-
identification and molecular characterization of 14 different enzyme mutations and 13 different polymorphic changes present in 10 mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
additional information
-
exploitation of alternative receptor systems that are independent of glycosylation but allow for efficient delivery to the lysosome, fusions of the human lysosomal enzyme with the receptor-associated protein, RAP, are efficiently endocytosed by lysosomal storage disorder patient fibroblasts, rat C6 glioma cells, mouse C2C12 myoblasts, and recombinant CHO cells expressing individual members of the low-density lipoprotein receptor family, uptake of the fusion exceeds that of phosphorylated enzyme in all cases, uptake is mediated by oligosaccharide receptors including the cation-independent mannose 6-phosphate receptor and the mannose receptor, and is specifically mediated by members of the low-density lipoprotein receptor protein family and is followed by delivery of the fusions to the lysosome, stability or recombinant fusion enzymes, overview
additional information
-
identification of naturally occurring mutations of residues Q70, W402, R268, Q400, Y343, W180 to premature stop codons, mutations are involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, natural stop codon read-through and clinical MPSI phenotype, overview
additional information
diverse missense mutations of the human enzyme's core, surface, and active site are correlated to the development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, structural implications, detailed overview
additional information
-
diverse missense mutations of the human enzyme's core, surface, and active site are correlated to the development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, structural implications, detailed overview
additional information
-
nonsense mutation of residue Q70 is involved in the disease mucopolysaccharidosis type I, MPSI, changes in hair morphology of MPSI patients treated with recombinant human enzyme in enzyme replacement therapy, overview
additional information
-
over 100 disease-causing IDUA mutations identified in patients with mucopolysaccharidosis type I. Most common mutations that introduce premature stop codons are p.W402X and p.Q70X. Deficient IDUA activity results in the accumulation of dermatan and heparan sulfate in urine of affected individuals
additional information
-
construction of a protein mutant AGT-181, that is a genetically engineered fusion protein of human iduronidase and a chimeric monoclonal antibody against the human insulin receptor. The mutant AG-181 is administered to Maccaca mulatta, chronic AGT-181 dosing does not result in toxicity at any dose, and causes no changes in organ histology, no change in plasma or cerebrospinal fluid glucose, and no significant immune response. AGT-181 is rapidly removed from plasma, but shows iduronidase enzyme activity
additional information
-
gene IDUA, screening and genotyping of nonsense, 4 missense, 1 deletion, and 2 splice site intron mutations in 10 MPS I patients, development and evaluation of a dHPLC screening method, overview
additional information
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder, phenotype with and without treatment with laronidase, overview
additional information
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder, phenotypes, overview. Growth patterns in terms of body height, weight, head and chest circumference in patients with MPS I without treatment and after enzyme replacement therapy with alpha-L-iduronidase, overview
additional information
-
ability of recombinant baby hamster kidney cells transfected with human IDUA cDNA in correcting skin fibroblasts from mucopolysaccharidosis I patients in vitro, after encapsulation in alginate microcapsules, overview. The cells use the mannose-6-phosphate receptor to internalize the recombinant enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
enzyme from mucopolysaccharidosis patients is more stable than enzyme from healthy individuals
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme activity significantly decayes starting at 21 days after the filter paper was impregnated with blood
the lysosomal (or tissue) half-life of recombinant human IDU appears to be approximately 6-7 days because a 3fold higher than normal enzyme level (300%) elevation is reduced to about 20% over a period of 28 days
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.03M sodium dimethylglutarate buffer, 10% glycerol, 0.5 M NaCl, pH 6 or 3.7, 18 months, 80% of activity retained
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Eshmuno S column chromatography and Toyopearl phenyl 650 M column chromatography
native and recombinant wild-type and mutant enzymes partially by immunoprecipitation
recombinant enzyme with and without a C-terminal ER-retention signal from seeds of Brassica napus and Nicotiana tabacum by lectinb affinity, immunoaffinity, and adsorption chromatography
-
recombinant wild-type enzyme and human receptor-associated protein RAP-fusion enzyme from LRP1-null CHO-K1 cells by heparin affinity and hydrophobic interaction chromatography, and gel fitration
-
the commercial preparation of recombinant enzyme expressed in CHO cells is further purified by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
commercially available recombinant human iduronidase (Aldurazyme) produced in Chinese-hamster-ovary cells
-
expression in Cos-1 cells
expression of IDUA with and without a C-terminal endoplasmic reticulum-retention sequence SEKDEL, in seeds of Brassica napus and Nicotiana tabacum under the control of regulatory 5'-, signal-peptide-encoding-, and 3'-sequences from the arcelin 5-I gene of Phaseolus vulgaris
-
expression of wild-type enzyme and enzyme in fusion with the human receptor-associated protein, RAP, in LRP1-null CHO-K1 cells
-
gene IDUA, screening and genotyping of nonsense, 4 missense, 1 deletion, and 2 splice site intron mutations in 10 MPS I patients, development and evaluation of a dHPLC screening method, overview
-
genotyping of different mucopolysaccharidosis type I patient cell lines, overview
-
IDUA cloning in Escherichia coli strain BL21, and overexpression in transgenic Nicotiana tabacum BY-2 cells, establishing and evaluation of the expression system, overview. A plant signal peptide is essential for proper expression and secretion of the glycosylated recombinant hIDUA into the cultured media of transgenic BY-2 cells, transfection by Agrobacterium tumefaciens, strain LBA4404
-
IDUA gene, determination of mutant sequences from mucopolysaccharidosis type I enzymes, genotyping, expression of wild-type and mutant enzymes in CHO cells
incorporated via mannose 6-phosphate receptors into human fibroblasts from a patient with MPS I (F17) or a healthy subject (F592), into cultured mouse osteoblasts (MC3T3-E1) or cultured mouse fibroblasts (F665)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
following three repeat intrathecal administrations of 0.1 mg/kg recombinant human alpha-L-iduronidase or placebo on days 1, 4 or 5, and 9, two days after the final intrathecal injection, the mean tissue alpha-L-iduronidase activity in the brains of the two treated animals are approximately 3times higher than the activity found in normal cat brains and remains higher than untreated mucopolysaccharidosis type I brain at 1 month before returning to near-baseline levels after 2 months
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
determining residual IDUA activity in fibroblasts of MPS I patients may be helpful to predict MPS I phenotype. Early recognition of the phenotype of MPS I patients is essential to timely initiate the most appropriate therapeutic strategy
drug development
-
mutant AGT-181 might be useful as a therapeutic approach to treatment of the brain in Hurlers syndrome
medicine
pharmacology
medicine
the enzyme is a target for enzyme replacement therapy of mucopolysaccharidosis type I patients
medicine
-
the enzyme is a target for enzyme replacement therapy of lysosomal storage disorders of mucopolysaccharidosis type I patients, the therapy depends on efficient uptake of recombinant enzyme into tissues of patients
medicine
-
the recombinant enzyme is used in enzyme relacement therapy of the Hurler form of mucopolysaccharidosis type I, MPSI, the enzyme is administered intraventricularly in to 31 Sprague-Dawley rat brains showing penetration of the brain and uptak into neurons and glial cells, rat tissue distribution of human recombinant enzyme activity, overview
medicine
-
administration of a high dose of the enzyme or development of a recombinant alpha-L-iduronidase containing many mannose 6-phosphate residues is required for further improvement of enzyme replacement therapy for skeletal disorders caused by mucopolysaccharidosis I
medicine
-
commercially available recombinant human laronidase (Aldurazyme) infusion is safe and effective in stabilizing or improving pulmonary function and physical endurance. Preclinical trials of the enzyme in the canine, dog and feline model and clinicial trials with affected patients with mucopolysaccharidosis type I
medicine
-
as there is a difference in IDUA structural change between the severe mucopolysaccharidosis type I group and the attenuated one, except for a couple of mutations, structural analysis can help predict the clinical outcome of the disease
medicine
-
the benefit of enzyme replacement therapy with recombinant laronidase before hematopoietic stem cell transplantation for mucopolysaccharidosis I is linked to improvement in patient's pretransplantation condition and thus tolerance of such intensive therapy. Short-term use of laronidase is not associated with increased risk of either graft-versus-host-disease or graft failure
medicine
-
currently approved laronidase dose regimen, to treat the lysosomal storage disorder mucopolysaccharidosis type I, has similar efficacy and potentially improved safety compared to regimens using higher doses, regardless of dose frequency. The approved 0.58 mg/kg/week laronidase dose regimen provides near-maximal reductions in glycosaminoglycan storage and the best benefit-to-risk ratio. The 1.2 mg/kg every 2 weeks regimen may be an acceptable alternative for patients with difficulty receiving weekly infusions, but the long-term effects of this regimen are unknown. In general, laronidase therapy is safe and well tolerated in all treatment groups
medicine
-
long-term clinical benefit and safety of laronidase in attenuated patients with mucopolysaccharidosis I. Laronidase effectively treats respiratory dysfunction, poor endurance, restricted mobility, hepatomegaly, and decreased quality of life. Prompt disease recognition and early and sustained treatment with laronidase will maximize these important benefits of treatment
medicine
-
effectiveness of enzyme replacement therapy with laronidase on the range of motion of upper extremities and influence on activities of daily living of patients with mucopolysaccharidosis type I, MPS I, overview. MPS I has a spectrum of clinical severity, and is subdivided into three phenotypes: Hurler syndrome, that is severe, Hurler-Scheie syndrome, that is intermediate, and Scheie syndrome, that is attenuated
medicine
-
the enzyme is useful in treatment of mucopolysaccharidosis type I, MPS I. In three patients with attenuated MPSA I, treated by laronidase, patients 2 and 3 display significant cognitive improvement within 2 years, and patients 1 and 3 display improvement, on MRI scans of the brain, overview
medicine
-
the enzyme is useful in treatment of mucopolysaccharidosis type I, MPS I, by enzyme replacement therapy
medicine
-
intrathecal administration of recombinant human IDU, with potential dosing every 2-3 months, may provide benefit for the treatment of central nervous system disease in mucopolysaccharidosis type I patients
medicine
-
intrathecal administration of recombinant human IDU, with potential dosing every 2-3 months, may provide benefit for the treatment of central nervous system disease in mucopolysaccharidosis type I patients
medicine
-
alpha-L-iduronidase is used in enzyme replacement therapy approved for mucopolysaccharidosis type I treatment
medicine
-
a clone overexpressing the enzyme and, after encapsulation in alginate microcapsules, correcting MPS I human skin fibroblasts.These capsules can be surgically implanted in sites which are difficult to reach such as the brain of animal models and can be an approach for the treatment of MPS I and other lysosomal storage disorders
pharmacology
-
exploitation of alternative receptor systems that are independent of glycosylation but allow for efficient delivery to the lysosome
pharmacology
-
the enzyme is used in enzyme replacement therapy of mucopolysaccharidosis type I, MPSI, changes in hair morphology of MPSI patients treated with recombinant human enzyme, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matalon, R.; Cifonelli, J.A.; Dorfmann, A.
L-Iduronidase in cultured human fibroblasts and liver
Biochem. Biophys. Res. Commun.
42
340-345
1971
Homo sapiens
brenda
Weissmann, B.; Santiago, R.
alpha-L-Iduronidase in lysosomal extracts
Biochem. Biophys. Res. Commun.
46
1430-1433
1972
Rattus norvegicus
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Hall, C.W.; Neufeld, E.F.
alpha-L-iduronidase activity in cultured skin fibroblasts and amniotic fluid cells
Arch. Biochem. Biophys.
158
817-821
1993
Homo sapiens
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Shapiro, L.J.; Hall, C.W.; Leder, I.G.; Neufeld, E.F.
The relationship of alpha-L-iduronidase and hurler corrective faktor
Arch. Biochem. Biophys.
172
156-161
1976
Homo sapiens
brenda
Rome, L.H.; Garvin, A.J.; Neufeld, E.F.
Human kidney alpha-L-iduronidase: purification and characterization
Arch. Biochem. Biophys.
189
344-353
1978
Homo sapiens
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Clements, P.R.; Brooks, D.A.; McCourt, P.A.G.; Hopwood, J.J.
Immunopurification and characterization of human alpha-L-iduronidase with the use of monoclonal antibodies
Biochem. J.
259
199-208
1989
Homo sapiens
brenda
Ohshita, T.; Sakuda, H.; Nakasone, S.; Iwamasa, T.
Purification, characterization and localization of pig liver alpha-L-iduronidase
Eur. J. Biochem.
179
201-207
1989
Sus scrofa
brenda
di Bello, I.C.; Dorling, P.; Fellows, L.; Winchester, B.
Specifc inhibition of human beta-D-glucuronidase and alpha-L-iduronidase by a trihydroxy pipecolic acid of plant origin
FEBS Lett.
176
61-64
1984
Homo sapiens
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Myerowitz R.; Neufeld, E.F.
Maturation of alpha-L-iduronidase in cultured human fibroblasts
J. Biol. Chem.
256
3044-3048
1981
Homo sapiens
brenda
Clements, P.R.; Brooks, D.A.; Saccone, G.T.P; Hopwood, J.J.
Human alpha-L-iduronidase. 1. purification, monoclonal antibody production, native and subunit molecular mass
Eur. J. Biochem.
152
21-28
1985
Homo sapiens
brenda
Clements, P.R.; Muller, V.; Hopwood, J.J.
Human alpha-L-iduronidase. 2. catalytic properties
Eur. J. Biochem.
152
29-34
1985
Homo sapiens
brenda
Schuchmann, E.H.; Astrin, K.H.; Aula, P.; Desnick, R.J.
Regional assignment of the structural gene for human alpha-L-iduronidase
Proc. Natl. Acad. Sci. USA
81
1169-1173
1984
Homo sapiens
brenda
Schuchmann, E.H.; Guzmann, N.A.; Desnick, R.J.
Human alpha-L-iduronidase. I. Purification and properties of the high uptake (higher molecular weight) and the low uptake (processed) forms
J. Biol. Chem.
259
3132-3140
1984
Homo sapiens
brenda
Rome, L.H.
alpha-L-Iduronidase from human kidney
Methods Enzymol.
83
578-583
1982
Homo sapiens
brenda
Kosaka, H.; Isemura, M.; Ono, T.; Nishimura, Y.; Kato, K.
Studies on the alpha-L-iduronidase activity of beta-glucuronidase preparations from bovine liver, rat liver, and rat preputial gland
J. Biochem.
88
69-75
1980
Bos taurus, Rattus norvegicus
brenda
Freeman, C.; Hopwood, J.J.
Human alpha-L-iduronidase. Catalytic properties and an integrated role in the lysosomal degradation of heparan sulphate
Biochem. J.
282
899-908
1992
Homo sapiens
brenda
Stoltzfus, L.J.; Sosa-Pineda, B.; Moskowitz, S.M.; Menon, K.P.; Dlott, B.; Hooper, L.; Teplow, D.B.; Shull, R.M.; Neufeld, E.F.
Cloning and characterization of cDNA encoding canine alpha-L-iduronidase
J. Biol. Chem.
267
6570-6575
1992
Canis sp.
brenda
Unger, E.G.; Durrant, J.; Anson, D.S.; Hopwood, J.J.
Recombinant alpha-L-iduronidase: characterization of the purified enzyme and correction of mucopolysaccharidosis type I fibroblasts
Biochem. J.
304
43-49
1994
Homo sapiens
brenda
Brooks, D.A.; Harper, G.S.; Gibson, G.J.; Ashton, L.J.; Taylor, J.A.; McCourt, P.A.D.; Freeman, C.; Clements, P.R.; Hoffmann, J.W.; Hopwood, J.J.
Hurler Syndrome: a patient with abnormally high levels of alpha-L-iduronidase
Biochem. Med. Metab. Biol.
47
211-220
1992
Homo sapiens
brenda
Kakkis, E.D.; Matynia, A.; Jonas, A.J.; Neufeld, E.F.
Overexpression of the human lysosomal enzyme alpha-L-iduronidase in chinese hamster ovary cells
Protein Expr. Purif.
5
225-232
1994
Homo sapiens
brenda
Stewart, K.; Brown, O.A.; Morelli, A.E.; Fairbairn, L.J.; Lashford, L.S.; Cooper, A.; Hatton, C.E.; Dexter, T.M.; Castro, M.G.; Lowenstein, P.R.
Uptake of alpha-(L)-iduronidase produced by retrovirally transduced fibroblasts into neuronal and glial cells in vitro
Gene Ther.
4
63-75
1997
Homo sapiens
brenda
Clarke, L.A.; Nasir, J.; Zhang, H.; McDonald, H.; Applegarth, D.A.; Hayden, M.R.; Toone, J.
Murine alpha-L-iduronidase: cDNA isolation and expression
Genomics
24
311-316
1994
Mus musculus
brenda
Sakuda, H.; Kusaba, A.; Ohshita, T.; Iwamasw, T.
Tissue and cellular distribution of alpha-L-iduronidase in the pig
J. Histochem. Cytochem.
38
785-792
1990
Sus scrofa
brenda
Ruth, L.; Eisenberg, D.; Neufeld, E.F.
alpha-L-Iduronidase forms semi-crystalline spherulites with amyloid-like properties
Acta Crystallogr. Sect. D
56
524-528
2000
Homo sapiens
-
brenda
Mandelli, J.; Wajner, A.; Pires, R.F.; Giugliani, R.; Coelho, J.C.
Detection of mucopolysaccharidosis type I heterozygotes based on the biochemical characteristics of leukocyte alpha-L-iduronidase
Arch. Med. Res.
33
20-24
2002
Homo sapiens
brenda
Nieman, C.E.; Wong, A.W.; He, S.; Clarke, L.; Hopwood, J.J.; Withers, S.G.
Family 39 alpha-L-iduronidases and beta-D-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile
Biochemistry
42
8054-8065
2003
Homo sapiens
brenda
Hein, L.K.; Hopwood, J.J.; Clements, P.R.; Brooks, D.A.
The alpha-L-iduronidase mutations R89Q and R89W result in an attenuated mucopolysaccharidosis type I clinical presentation
Biochim. Biophys. Acta
1639
95-103
2003
Homo sapiens
brenda
Mandelli, J.; Wajner, A.; Pires, R.; Giugliani, R.; Coelho, J.C.
Effect of CuCl2, NaCl and EDTA on the enzyme alpha-L-iduronidase in the plasma of normal individuals and heterozygotes for MPS I
Clin. Chim. Acta
318
83-89
2002
Homo sapiens
brenda
Brooks, D.A.; Fabrega, S.; Hein, L.K.; Parkinson, E.J.; Durand, P.; Yogalingam, G.; Matte, U.; Giugliani, R.; Dasvarma, A.; Eslahpazire, J.; Henrissat, B.; Mornon, J.P.; Hopwood, J.J.; Lehn, P.
Glycosidase active site mutations in human alpha-L-iduronidase
Glycobiology
11
741-750
2001
Homo sapiens
brenda
Kloska, A.; Bohdanowicz, J.; Konopa, G.; Tylki-Szym?ska, A.; Jakobkiewicz-Banecka, J.; Czartoryska, B.; Liberek, A.; Wegrzyn, A.; Wegrzyn, G.
Changes in hair morphology of mucopolysaccharidosis I patients treated with recombinant human alpha-L-iduronidase (laronidase, Aldurazyme)
Am. J. Med. Genet. A
139
199-203
2005
Homo sapiens
brenda
Yogalingam, G.; Guo, X.H.; Muller, V.J.; Brooks, D.A.; Clements, P.R.; Kakkis, E.D.; Hopwood, J.J.
Identification and molecular characterization of alpha-L-iduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
Hum. Mutat.
24
199-207
2004
Homo sapiens (P35475), Homo sapiens
brenda
Prince, W.S.; McCormick, L.M.; Wendt, D.J.; Fitzpatrick, P.A.; Schwartz, K.L.; Aguilera, A.I.; Koppaka, V.; Christianson, T.M.; Vellard, M.C.; Pavloff, N.; Lemontt, J.F.; Qin, M.; Starr, C.M.; Bu, G.; Zankel, T.C.
Lipoprotein receptor binding, cellular uptake, and lysosomal delivery of fusions between the receptor-associated protein (RAP) and alpha-L-iduronidase or acid alpha-glucosidase
J. Biol. Chem.
279
35037-35046
2004
Homo sapiens
brenda
Laradi, S.; Tukel, T.; Erazo, M.; Shabbeer, J.; Chkioua, L.; Khedhiri, S.; Ferchichi, S.; Chaabouni, M.; Miled, A.; Desnick, R.J.
Mucopolysaccharidosis I: alpha-L-iduronidase mutations in three tunisian families
J. Inherit. Metab. Dis.
28
1019-1026
2005
Homo sapiens
brenda
Hein, L.K.; Bawden, M.; Muller, V.J.; Sillence, D.; Hopwood, J.J.; Brooks, D.A.
alpha-L-Iduronidase premature stop codons and potential read-through in mucopolysaccharidosis type I patients
J. Mol. Biol.
338
453-462
2004
Homo sapiens
brenda
Rempel, B.P.; Clarke, L.A.; Withers, S.G.
A homology model for human alpha-L-iduronidase: insights into human disease
Mol. Genet. Metab.
85
28-37
2005
Homo sapiens (P35475), Homo sapiens
brenda
Belichenko, P.V.; Dickson, P.I.; Passage, M.; Jungles, S.; Mobley, W.C.; Kakkis, E.D.
Penetration, diffusion, and uptake of recombinant human alpha-L-iduronidase after intraventricular injection into the rat brain
Mol. Genet. Metab.
86
141-149
2005
Homo sapiens
brenda
Pabba, J.; Rempel, B.P.; Withers, S.G.; Vasella, A.
Synthesis of glycaro-1,5-lactams and tetrahydrotetrazolopyridine-5-carboxylates: inhibitors of beta-D-glucuronidase and alpha-L-iduronidase
Helv. Chim. Acta
89
635-666
2006
Homo sapiens
-
brenda
Di Domenico, C.; Di Napoli, D.; Gonzalez Y. Reyero, E.; Lombardo, A.; Naldini, L.; Di Natale, P.
Limited transgene immune response and long-term expression of human alpha-L-iduronidase in young adult mice with mucopolysaccharidosis type I by liver-directed gene therapy
Hum. Gene Ther.
17
1112-1121
2006
Homo sapiens
brenda
Wang, D.; Worsham, D.N.; Pan, D.
Co-expression of MGMT(P140K) and alpha-L-iduronidase in primary hepatocytes from mucopolysaccharidosis type I mice enables efficient selection with metabolic correction
J. Gene Med.
10
249-259
2008
Mus musculus
brenda
Chen, F.; Vitry, S.; Hocquemiller, M.; Desmaris, N.; Ausseil, J.; Heard, J.M.
Alpha-L-iduronidase transport in neurites
Mol. Genet. Metab.
87
349-358
2006
Homo sapiens
brenda
Chung, S.; Ma, X.; Liu, Y.; Lee, D.; Tittiger, M.; Ponder, K.P.
Effect of neonatal administration of a retroviral vector expressing alpha-L-iduronidase upon lysosomal storage in brain and other organs in mucopolysaccharidosis I mice
Mol. Genet. Metab.
90
181-192
2007
Homo sapiens
brenda
Wraith, J.E.; Beck, M.; Lane, R.; van der Ploeg, A.; Shapiro, E.; Xue, Y.; Kakkis, E.D.; Guffon, N.
Enzyme replacement therapy in patients who have mucopolysaccharidosis I and are younger than 5 years: results of a multinational study of recombinant human alpha-L-iduronidase (laronidase)
Pediatrics
120
e37-e46
2007
Homo sapiens
brenda
Downing, W.L.; Galpin, J.D.; Clemens, S.; Lauzon, S.M.; Samuels, A.L.; Pidkowich, M.S.; Clarke, L.A.; Kermode, A.R.
Synthesis of enzymatically active human alpha-L-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds
Plant Biotechnol. J.
4
169-181
2006
Homo sapiens
brenda
Kermode, A.R.; Zeng, Y.; Hu, X.; Lauson, S.; Abrams, S.R.; He, X.
Ectopic expression of a conifer Abscisic Acid Insensitive3 transcription factor induces high-level synthesis of recombinant human alpha-L-iduronidase in transgenic tobacco leaves
Plant Mol. Biol.
63
763-776
2007
Homo sapiens (P35475), Homo sapiens
brenda
Tsukimura, T.; Tajima, Y.; Kawashima, I.; Fukushige, T.; Kanzaki, T.; Kanekura, T.; Ikekita, M.; Sugawara, K.; Suzuki, T.; Togawa, T.; Sakuraba, H.
Uptake of a recombinant human alpha-L-iduronidase (laronidase) by cultured fibroblasts and osteoblasts
Biol. Pharm. Bull.
31
1691-1695
2008
Homo sapiens
brenda
Pastores, G.M.
Laronidase (Aldurazyme): enzyme replacement therapy for mucopolysaccharidosis type I
Expert. Opin. Biol. Ther.
8
1003-1009
2008
Homo sapiens
brenda
Sugawara, K.; Saito, S.; Ohno, K.; Okuyama, T.; Sakuraba, H.
Structural study on mutant alpha-L-iduronidases: insight into mucopolysaccharidosis type I
J. Hum. Genet.
53
467-474
2008
Homo sapiens
brenda
Wynn, R.F.; Mercer, J.; Page, J.; Carr, T.F.; Jones, S.; Wraith, J.E.
Use of enzyme replacement therapy (Laronidase) before hematopoietic stem cell transplantation for mucopolysaccharidosis I: experience in 18 patients
J. Pediatr.
154
135-139
2009
Homo sapiens
brenda
Giugliani, R.; Rojas, V.M.; Martins, A.M.; Valadares, E.R.; Clarke, J.T.; Goes, J.E.; Kakkis, E.D.; Worden, M.A.; Sidman, M.; Cox, G.F.
A dose-optimization trial of laronidase (Aldurazyme) in patients with mucopolysaccharidosis I
Mol. Genet. Metab.
96
13-19
2009
Homo sapiens
brenda
Clarke, L.A.; Wraith, J.E.; Beck, M.; Kolodny, E.H.; Pastores, G.M.; Muenzer, J.; Rapoport, D.M.; Berger, K.I.; Sidman, M.; Kakkis, E.D.; Cox, G.F.
Long-term efficacy and safety of laronidase in the treatment of mucopolysaccharidosis I
Pediatrics
123
229-240
2009
Homo sapiens
brenda
Kasper, D.C.; Iqbal, F.; Dvorakova, L.; Zeman, J.; Magner, M.; Bodamer, O.; Pollak, A.; Herkner, K.R.; Item, C.B.
Rapid and accurate denaturating high performance liquid chromatography protocol for the detection of alpha-L-iduronidase mutations causing mucopolysaccharidosis type I
Clin. Chim. Acta
411
345-350
2010
Homo sapiens
brenda
Boado, R.J.; Hui, E.K.; Lu, J.Z.; Pardridge, W.M.
AGT-181: expression in CHO cells and pharmacokinetics, safety, and plasma iduronidase enzyme activity in Rhesus monkeys
J. Biotechnol.
144
135-141
2009
Homo sapiens
brenda
Tylki-Szymanska, A.; Marucha, J.; Jurecka, A.; Syczewska, M.; Czartoryska, B.
Efficacy of recombinant human alpha-L-iduronidase (laronidase) on restricted range of motion of upper extremities in mucopolysaccharidosis type I patients
J. Inherit. Metab. Dis.
33
151-157
2010
Homo sapiens
brenda
Valayannopoulos, V.; Boddaert, N.; Barbier, V.; Le Merrer, M.; Caillaud, C.; de Lonlay, P.
Cognitive and neuroradiological improvement in three patients with attenuated MPS I treated by laronidase
Mol. Genet. Metab.
100
20-23
2010
Homo sapiens
brenda
Tylki-Szymanska, A.; Rozdzynska, A.; Jurecka, A.; Marucha, J.; Czartoryska, B.
Anthropometric data of 14 patients with mucopolysaccharidosis I: retrospective analysis and efficacy of recombinant human alpha-L-iduronidase (laronidase)
Mol. Genet. Metab.
99
10-17
2010
Homo sapiens
brenda
Fu, L.; Miao, Y.; Lo, S.; Seto, T.; Sun, S.; Xu, Z.; Clemens, S.; Clarke, L.; Kermode, A.; Jiang, L.
Production and characterization of soluble human lysosomal enzyme alpha-iduronidase with high activity from culture media of transgenic tobacco BY-2 cells
Plant Sci.
177
668-675
2009
Homo sapiens
-
brenda
Galpin, J.; Clemens, S.; Kermode, A.
The carboxy-terminal ER-retention motif, SEKDEL, influences the N-linked glycosylation of recombinant human alpha-L-iduronidase but has little effect on enzyme activity in seeds of Brassica napus and Nicotiana tabacum
Plant Sci.
178
440-447
2010
Homo sapiens
-
brenda
Sun, L.; Li, C.; Song, X.; Zheng, N.; Zhang, H.; Dong, G.
Three novel alpha-L-iduronidase mutations in 10 unrelated Chinese mucopolysaccharidosis type I families
Genet. Mol. Biol.
34
195-200
2011
Homo sapiens
brenda
Vite, C.H.; Wang, P.; Patel, R.T.; Walton, R.M.; Walkley, S.U.; Sellers, R.S.; Ellinwood, N.M.; Cheng, A.S.; White, J.T.; ONeill, C.A.; Haskins, M.
Biodistribution and pharmacodynamics of recombinant human alpha-L-iduronidase (rhIDU) in mucopolysaccharidosis type I-affected cats following multiple intrathecal administrations
Mol. Genet. Metab.
103
268-274
2011
Homo sapiens, Felis catus
brenda
Maita, N.; Taniguchi, H.; Sakuraba, H.
Crystallization, X-ray diffraction analysis and SIRAS phasing of human alpha-L-iduronidase
Acta Crystallogr. Sect. F
68
1363-1366
2012
Homo sapiens (P35475)
brenda
Lu, F.; Lico, L.; Hung, S.
Synthesis of a fluorogenic substrate for alpha-L-iduronidase
Arkivoc
2013
13-21
2012
Homo sapiens
-
brenda
Baldo, G.; Quoos Mayer, F.; Burin, M.; Carrillo-Farga, J.; Matte, U.; Giugliani, R.
Recombinant encapsulated cells overexpressing alpha-L-iduronidase correct enzyme deficiency in human mucopolysaccharidosis type I cells
Cells Tissues Organs
195
323-329
2012
Homo sapiens
brenda
Jung, G.; Pabst, M.; Neumann, L.; Berger, A.; Lubec, G.
Characterization of alpha-L-iduronidase (Aldurazyme) and its complexes
J. Proteomics
80
26-33
2013
Homo sapiens
brenda
Oussoren, E.; Keulemans, J.; van Diggelen, O.P.; Oemardien, L.F.; Timmermans, R.G.; van der Ploeg, A.T.; Ruijter, G.J.
Residual alpha-L-iduronidase activity in fibroblasts of mild to severe mucopolysaccharidosis type I patients
Mol. Genet. Metab.
109
377-381
2013
Homo sapiens
brenda
Ou, L.; Herzog, T.L.; Wilmot, C.M.; Whitley, C.B.
Standardization of alpha-L-iduronidase enzyme assay with Michaelis-Menten kinetics
Mol. Genet. Metab.
111
113-115
2014
Mus musculus, Mus musculus C57BL/6
brenda
Maita, N.; Tsukimura, T.; Taniguchi, T.; Saito, S.; Ohno, K.; Taniguchi, H.; Sakuraba, H.
Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module
Proc. Natl. Acad. Sci. USA
110
14628-14633
2013
Homo sapiens
brenda
Cheng, W.C.; Lin, C.K.; Li, H.Y.; Chang, Y.C.; Lu, S.J.; Chen, Y.S.; Chang, S.Y.
A combinatorial approach towards the synthesis of non-hydrolysable triazole-iduronic acid hybrid inhibitors of human alpha-L-iduronidase discovery of enzyme stabilizers for the potential treatment of MPSI
Chem. Commun. (Camb.)
54
2647-2650
2018
Homo sapiens (P35475)
brenda
Artola, M.; Kuo, C.L.; McMahon, S.A.; Oehler, V.; Hansen, T.; van der Lienden, M.; He, X.; van den Elst, H.; Florea, B.I.; Kermode, A.R.; van der Marel, G.A.; Gloster, T.M.; Codee, J.D.C.; Overkleeft, H.S.; Aerts, J.M.F.G.
New irreversible alpha-L-iduronidase inhibitors and activity-based probes
Chemistry
24
19081-19088
2018
Homo sapiens (P35475), Homo sapiens
brenda
Breier, A.C.; Ce, J.; Mezzalira, J.; Daitx, V.V.; Moraes, V.C.; Goldim, M.P.S.; Coelho, J.C.
alpha-L-iduronidase and arylsulfatase B in dried blood spots on filter paper Biochemical parameters and time stability
Clin. Biochem.
50
431-435
2017
Homo sapiens (P35475)
brenda
Cardon, F.; Pallisse, R.; Bardor, M.; Caron, A.; Vanier, J.; Ele Ekouna, J.P.; Lerouge, P.; Boitel-Conti, M.; Guillet, M.
Brassica rapa hairy root based expression system leads to the production of highly homogenous and reproducible profiles of recombinant human alpha-L-iduronidase
Plant Biotechnol. J.
17
505-516
2019
Homo sapiens (P35475), Homo sapiens
brenda
Liu, D.; Jiang, Z.; Deng, L.; Li, H.; Jiang, H.
Identification of an alpha-L-iduronidase (IDUA) M1T mutation in a Chinese family with autosomal recessive mucopolysaccharidosis I
Ann. N. Y. Acad. Sci.
1526
114-125
2023
Homo sapiens (P35475)
brenda
Ngiwsara, L.; Sawangareetrakul, P.; Wattanasirichaigoon, D.; Tim-Aroon, T.; Dejkhamron, P.; Champattanachai, V.; Ketudat-Cairns, J.R.; Svasti, J.
Effects of gentamicin inducing readthrough premature stop Codons A study of alpha-L-iduronidase nonsense variants in COS-7 Cells
Biochem. Biophys. Res. Commun.
636
147-154
2022
Homo sapiens (P35475)
brenda
Doherty, G.G.; Ler, G.J.M.; Wimmer, N.; Bernhardt, P.V.; Ashmus, R.A.; Vocadlo, D.J.; Armstrong, Z.; Davies, G.J.; Maccarana, M.; Li, J.P.; Kayal, Y.; Ferro, V.
Synthesis of uronic acid 1-azasugars as putative inhibitors of alpha-iduronidase, beta-glucuronidase and heparanase
ChemBioChem
24
e202200619
2023
Homo sapiens (P35475)
brenda
Lin, H.Y.; Chang, S.Y.; Teng, H.H.; Wu, H.J.; Li, H.Y.; Cheng, C.C.; Chuang, C.K.; Lin, H.Y.; Lin, S.P.; Cheng, W.C.
Discovery of small-molecule protein stabilizers toward exogenous alpha-L-iduronidase to reduce the accumulated heparan sulfate in mucopolysaccharidosis type I cells
Eur. J. Med. Chem.
247
115005
2023
Homo sapiens (P35475)
brenda
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