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1-naphthyl sulfate + H2O
1-naphthol + sulfate
-
-
-
-
?
1-O-alkyl-2-O-acyl-3-(beta-3'-sulfogalactosyl)glycerol + H2O
1-O-alkyl-2-O-acyl-3-O-(beta-galactosyl)glycerol + sulfate
1-O-alkyl-2-O-acyl-3-O-(beta-D-galactopyranoside-3'-sulfate)-glycerol + H2O
1-O-alkyl-2-O-acyl-3-O-beta-D-galactopyranoside-glycerol + sulfate
-
-
-
-
?
1-O-hexadecyl-2-O-hexadecanoyl-3-O-(beta-3'-sulfogalactosyl)glycerol + H2O
1-O-hexadecyl-2-O-hexadecanoyl-3-O-(beta-galactosyl)glycerol + sulfate
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
2-hydroxyphenyl sulfate + H2O
2-hydroxyphenol + sulfate
-
-
-
-
?
2-naphthyl sulfate + H2O
2-naphthol + sulfate
-
-
-
-
?
2-nitrophenyl sulfate + H2O
2-nitrophenol + sulfate
-
-
-
-
?
2-nitropyridyl 3-sulfate + H2O
2-nitropyridin-3-ol + sulfate
-
-
-
-
?
3-nitrophenyl sulfate + H2O
3-nitrophenol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
5,6,7,8-tetrahydro-2-naphthyl sulfate + H2O
5,6,7,8-tetrahydro-2-naphthol + sulfate
-
-
-
-
?
ascorbate 2-sulfate + H2O
ascorbate + sulfate
cerebroside 3-sulfate + H2O
cerebroside + sulfate
cerebroside 3-sulphate + H2O
cerebroside + sulfate
the enzyme catalyzes the first step in the degradation of the glycolipid cerebroside sulfate
-
?
chondroitin sulfate B + H2O
sulfate
-
-
-
-
?
dehydroisoandrosterone sulfate + H2O
dehydroisoandrosterone + sulfate
-
-
-
-
?
estriol 3-sulfate + H2O
estriol + sulfate
-
-
-
-
?
estrone 3-sulfate + H2O
estrone + sulfate
-
-
-
-
?
galactose(3-sulfate)beta1-1'(N-2-hydroxy-acyl)sphingosine + H2O
galactose beta1-1'(N-2-hydroxy-acyl)sphingosine + sulfate
-
-
-
-
?
hyaluronan + H2O
?
-
-
-
-
?
lysoseminolipid sulfate + H2O
lysoseminolipid + sulfate
-
deacylated seminolipid
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
N-acyl-1-O-(beta-3-sulfogalactosyl)sphingosine + H2O
(N-acyl-1-O-galactosyl) sphingosine + sulfate
-
sulfosphingolipids
-
-
?
N-lissamine rhodaminyl-(12-aminododecanoyl)cerebroside 3-sulfate + H2O
?
-
-
-
-
?
naphthyl sulfate + H2O
naphthol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
phenanthryl sulfate + H2O
phenanthrol + sulfate
-
-
-
-
?
phenyl sulfate + H2O
phenol + sulfate
-
-
-
-
?
psychosine sulfate + H2O
psychosine + sulfate
-
deacylated sulphatide
-
-
?
pyridyl 3-sulfate + H2O
pyridol + sulfate
-
-
-
-
?
pyridyl 4-sulfate + H2O
pyridol + sulfate
-
-
-
-
?
seminolipid + H2O
galactolipid + sulfate
-
-
-
-
?
sulfogalactosylceramide + H2O
?
sulfogalactosylglycerolipid + H2O
?
tyrosine O-sulfate + H2O
tyrosine + sulfate
-
-
-
-
?
additional information
?
-
1-O-alkyl-2-O-acyl-3-(beta-3'-sulfogalactosyl)glycerol + H2O
1-O-alkyl-2-O-acyl-3-O-(beta-galactosyl)glycerol + sulfate
-
-
-
-
?
1-O-alkyl-2-O-acyl-3-(beta-3'-sulfogalactosyl)glycerol + H2O
1-O-alkyl-2-O-acyl-3-O-(beta-galactosyl)glycerol + sulfate
-
seminolipid, sulfoglycerolipids
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
artificial substrate, Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
artificial substrate, Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
ascorbate 2-sulfate + H2O
ascorbate + sulfate
-
-
-
-
?
ascorbate 2-sulfate + H2O
ascorbate + sulfate
-
-
-
-
?
ascorbate 2-sulfate + H2O
ascorbate + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
Blaberus fuscus
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
135666, 135667, 135668, 135669, 135670, 135671, 135672, 135676, 135677, 135678, 135681, 135686, 135687, 135691, 135695, 649125 -
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
galactosyl ceramid
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
galactosyl ceramide
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
activity depends on ionic strength
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
no requirement for activators when acting on cerebroside sulfate
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
3-O-sulfogalactosyl ceramide
galactosyl ceramide
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
the enzyme catalyzes the first step in the degradation of the glycolipid cerebroside sulfate. Accumulation of cerebroside sulfate is responsible for metachromatic leukodystrophy, a severe autosomal recessive inherited disorder. Good correlation between the type of mutation, deficient arylsulfatase A activity and disease severity is recognized
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
the reaction requires saposin B, a non-enzymatic proteinaceous cofactor which presents sulfatide to the catalytic site of arylsulfatase A, desulfation is negligible when Sap B is substituted by Sap A, C, or D
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
-
-
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
-
-
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
Blaberus fuscus
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
-
-
-
?
sulfogalactosylceramide + H2O
?
-
-
-
?
sulfogalactosylceramide + H2O
?
Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
sulfogalactosylceramide + H2O
?
-
-
-
?
sulfogalactosylceramide + H2O
?
Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
sulfogalactosylglycerolipid + H2O
?
-
-
-
?
sulfogalactosylglycerolipid + H2O
?
Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
sulfogalactosylglycerolipid + H2O
?
-
-
-
-
?
sulfogalactosylglycerolipid + H2O
?
-
-
-
?
sulfogalactosylglycerolipid + H2O
?
Cys69 is the catalytic residue, and Lys302 and Lys123 act as residues anchoring the sulfate group to the active site, interaction with the enzyme active site, overview
-
-
?
additional information
?
-
-
metachromatic leukodystrophy is a lysosomal storage disorder caused by the deficiency of enzyme
-
-
?
additional information
?
-
substrate binding and docking study, using crystal structures, PDB IDs 1N2K and 1E2S, overview
-
-
?
additional information
?
-
recombinant mouse ArsA tightly binds to sulfated polysaccharides
-
-
?
additional information
?
-
-
AS-A has mannose, N-acetylglucosamine and/or sialic acid residues as part of its glycosilation
-
-
?
additional information
?
-
-
is able to disperse cumulus layers of cumulus oocyte complexes. Chondroitin sulfate A, chondroitin sulfate C, ovalbumin and heparan sulfate do not show interaction with AS-A
-
-
?
additional information
?
-
substrate binding and docking study, using human crystal structures, PDB IDs 1N2K and 1E2S, overview
-
-
?
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Adrenoleukodystrophy
Bone marrow-derived mesenchymal stem cells remain host-derived despite successful hematopoietic engraftment after allogeneic transplantation in patients with lysosomal and peroxisomal storage diseases.
arylsulfatase (type i) deficiency
Multiple sulfatase deficiency with a novel biochemical presentation.
arylsulfatase (type i) deficiency
Retinal pigment epithelial degeneration associated with leukocytic arylsulfatase A deficiency.
Breast Diseases
Evaluation of leukocyte arylsulfatase-A activity in patients with breast cancer and benign breast disease.
Breast Neoplasms
Evaluation of leukocyte arylsulfatase-A activity in patients with breast cancer and benign breast disease.
Cerebral Palsy
Kinetics and activity of arylsulfatase A in leukocytes derived from patients with cerebral palsy.
cerebroside-sulfatase deficiency
Complications in the genotypic molecular diagnosis of pseudo arylsulfatase A deficiency.
cerebroside-sulfatase deficiency
Deficient glycosylation of arylsulfatase A in pseudo arylsulfatase-A deficiency.
cerebroside-sulfatase deficiency
Metachromatic leukodystrophy: arylsulfatase-A deficiency in skin fibroblast cultures.
cerebroside-sulfatase deficiency
Pseudo arylsulfatase-A deficiency in healthy individuals: genetic and biochemical relationship to metachromatic leukodystrophy.
Cranial Nerve Diseases
Isolated cranial nerve enhancement in metachromatic leukodystrophy.
Demyelinating Diseases
Delayed postanoxic demyelination and arylsulfatase-A pseudodeficiency.
Gait Disorders, Neurologic
Isolated cranial nerve enhancement in metachromatic leukodystrophy.
Leukodystrophy, Globoid Cell
Late-onset Krabbe disease initially diagnosed as cerebroside sulfatase activator deficiency.
Leukodystrophy, Metachromatic
A correlation of intracellular cerebroside sulfatase activity in fibroblasts with latency in metachromatic leukodystrophy.
Leukodystrophy, Metachromatic
Adult metachromatic leukodystrophy. II. Ultrastructural findings in peripheral nerve and skeletal muscle.
Leukodystrophy, Metachromatic
An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy.
Leukodystrophy, Metachromatic
Arylsulfatases A and B in EBV-transformed lymphoid cell lines: studies on their molecular forms in cells from patients with inborn sulfatase deficiencies. Comparative diagnostic value of enzymatic assays.
Leukodystrophy, Metachromatic
Autoreactivity to Sulfatide by Human Invariant NKT Cells.
Leukodystrophy, Metachromatic
Biochemical characterization of two (C300F, P425T) arylsulfatase a missense mutations.
Leukodystrophy, Metachromatic
Cerebroside sulfatase activator deficiency induced metachromatic leukodystrophy.
Leukodystrophy, Metachromatic
Cerebroside sulfatase activity in cultivated human skin fibroblasts and amniotic fluid cells;.
Leukodystrophy, Metachromatic
Correction of Brain Oligodendrocytes by AAVrh.10 Intracerebral Gene Therapy in Metachromatic Leukodystrophy Mice.
Leukodystrophy, Metachromatic
Deficient glycosylation of arylsulfatase A in pseudo arylsulfatase-A deficiency.
Leukodystrophy, Metachromatic
Diffuse-disseminated sclerosis combined with partial arylsulfatase A (ASA) deficiency. Mixed heterozygosity of ASA- and pseudo-ASA-deficiency?
Leukodystrophy, Metachromatic
Discussion: Metachromatic leukodystrophy, an unusual case with a subtle cerebroside sulfatase defect.
Leukodystrophy, Metachromatic
Genetic complementation in somatic cell hybrids of cerebroside sulfatase activator deficiency and metachromatic leukodystrophy fibroblasts.
Leukodystrophy, Metachromatic
Improved synthesis of [1-14C]acyl-sphingosine-galactose-3-sulfate (sulfatide) for diagnosis of metachromatic leukodystrophy: usefulness of radioscanning.
Leukodystrophy, Metachromatic
Late-Onset Metachromatic Leukodystrophy with Early Onset Dementia Associated with a Novel Missense Mutation in the Arylsulfatase A Gene.
Leukodystrophy, Metachromatic
Metachromatic leukodystrophy caused by a partial cerebroside sulfatase.
Leukodystrophy, Metachromatic
Metachromatic leukodystrophy. Diffusion MR imaging and proton MR spectroscopy.
Leukodystrophy, Metachromatic
Metachromatic leukodystrophy. Treatment with arylsulfatase-A.
Leukodystrophy, Metachromatic
Metachromatic leukodystrophy: arylsulfatase-A deficiency in skin fibroblast cultures.
Leukodystrophy, Metachromatic
Metachromatic leukodystrophy: molecular genetics and an animal model.
Leukodystrophy, Metachromatic
Molecular and clinical consequences of novel mutations in the arylsulfatase A gene.
Leukodystrophy, Metachromatic
Multiple sulfatase deficiency with a novel biochemical presentation.
Leukodystrophy, Metachromatic
Prenatal diagnosis of metachromatic leukodystrophy: a diagnosis by amniotic fluid and its confirmation.
Leukodystrophy, Metachromatic
Pseudo arylsulfatase-A deficiency in healthy individuals: genetic and biochemical relationship to metachromatic leukodystrophy.
Leukodystrophy, Metachromatic
Pseudodeficiency of arylsulphatase A: strategy for clarification of genotype in families of subjects with low ASA activity and neurological symptoms.
Leukodystrophy, Metachromatic
Retinal pigment epithelial degeneration associated with leukocytic arylsulfatase A deficiency.
Leukodystrophy, Metachromatic
The AB-variant of metachromatic leukodystrophy (postulated activator protein deficiency). Light and electron microscopic findings in a sural nerve biopsy.
Leukodystrophy, Metachromatic
Very low arylsulfatase A and cerebroside sulfatase activities in leukocytes of healthy members of metachromatic leukodystrophy family.
Leukodystrophy, Metachromatic
[Metachromatic leucodystrophy. Clinical, biological, and therapeutic aspects]
Leukodystrophy, Metachromatic
[Problems in the diagnosis of metachromatic leukodystrophy by arylsulfatase-A assay in white blood cells. Genetic study of normal enzyme values in 64 mother and child pairs (author's transl)]
Lysosomal Storage Diseases
Biochemical characterization of two (C300F, P425T) arylsulfatase a missense mutations.
Lysosomal Storage Diseases
Deficient glycosylation of arylsulfatase A in pseudo arylsulfatase-A deficiency.
Lysosomal Storage Diseases
[Metachromatic leucodystrophy. Clinical, biological, and therapeutic aspects]
Multiple Sclerosis
Brain galactolipid content in a patient with pseudoarylsulfatase A deficiency and coincidental diffuse disseminated sclerosis, and in patients with metachromatic, adreno-, and other leukodystrophies.
Multiple Sulfatase Deficiency Disease
Multiple sulfatase deficiency with a novel biochemical presentation.
Neoplasms
Determination of diagnostic and prognostic values of urinary interleukin-8, tumor necrosis factor-alpha, and leukocyte arylsulfatase-A activity in patients with bladder cancer.
Neurodegenerative Diseases
Pseudo arylsulfatase-A deficiency in healthy individuals: genetic and biochemical relationship to metachromatic leukodystrophy.
Urinary Bladder Neoplasms
Determination of diagnostic and prognostic values of urinary interleukin-8, tumor necrosis factor-alpha, and leukocyte arylsulfatase-A activity in patients with bladder cancer.
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A212P
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
A96G
mutation contributes to enzyme activity reduction
C168stop
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
C300F
-
the sequence alteration is found in a patient with metachromatic leukodystrophy, the mutant strongly interferes with the octamerization process of enzyme but not with its dimerization capacity
C493F
mutant shows 0.7% of wild type ARSA activity
C69A
The inactive mutant in complex with p-nitrocatechol sulfate mimics a reaction intermediate during sulfate ester hydrolysis by the active enzyme, without the covalent bond to the key side-chain C-alpha-formylglycine
D255H
-
inactive misfolded mutant D255H-ASA
D335V
-
inactive misfolded mutant D335V-ASA
D407fs
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
E253K
mutation contributes to enzyme activity reduction
E253K/T391S
mutations contribute to sum of the enzyme activity reduction ascribed to each mutation
E307K
naturally occuring ARSA polymorphism, causes a mild peripheral neuropathy phenotype
G293C
mutant shows 0.5% of wild type ARSA activity
G86D
-
inactive misfolded mutant G86D-ASA
H138D
naturally occuring ARSA polymorphism, causes a mild peripheral neuropathy phenotype
H231Q
mutation identified in three patients belonging to a consanguineous family with late-infantile metachromatic leukodystrophy disorder MLD. The mutation leads to changes in the pre-mRNA secondary structure and in the ArsA protein structure
L52P
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
P136L
-
inactive misfolded mutant P136LASA
P377L
-
inactive misfolded mutant P377L-pdASA
P425T
-
the sequence alteration is found in a patient with metachromatic leukodystrophy, the mutant displays a modest reduction of oligomerization process but not with its dimerization capacity
P426L
mutation contributes to enzyme activity reduction
P426L/N350S/96A>G
mutations contribute to sum of the enzyme activity reduction ascribed to each mutation
R288H/R496H/N350S
-
about 38% reduction of enzyme activity in comparison to wild-type enzyme, no additive effect of the various amino acid substitutions is found in vitro
S406G
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
T201C
-
inactive misfolded mutant T201C-ASA
T275M
-
inactive misfolded mutant T275M-ASA
T304M
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
T391S
mutation contributes to enzyme activity reduction
C69A
site-directed mutagenesis, the mnutant shows abolished enzyme activity and only residual binding to thr sulfoglycolipid substrate
C69A/K123A/K302A
site-directed mutagenesis, the mutant shows abolished substrate binding and activity
C500F
-
about 8% reduction of enzyme activity in comparison to wild-type enzyme
C500F
-
about 8% reduction of enzyme activity in comparison to wild-type enzyme. Mutation found in a patient with metachromatic leukodystrophy
C69S
the mutant is able to bind covalently to the substrate and hydrolyse it, but is unable to release the resulting sulfate
C69S
present at significantly higher levels in both conditioned media and within the cell when compared with wild type
E382Q
-
complete loss of enzyme activity in comparison to wild-type enzyme in vitro
E382Q
-
complete loss of enzyme activity in comparison to wild-type enzyme in vitro. Mutation found in a patient with metachromatic leukodystrophy
K302A
-
34% enzyme activity in comparison to wild-type enzyme
K302A
-
34% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium
K367A
-
60% enzyme activity in comparison to wild-type enzyme
K367A
-
60% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 106% of the mannose-phosphorylation of the wild-type enzyme
K393A
-
39% enzyme activity in comparison to wild-type enzyme
K393A
-
39% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 123% of the mannose-phosphorylation of the wild-type enzyme
K393A/K395G
-
35% enzyme activity in comparison to wild-type enzyme
K393A/K395G
-
35% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium
K393A/K395H
-
30% enzyme activity in comparison to wild-type enzyme
K393A/K395H
-
30% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium
K433A
-
102% enzyme activity in comparison to wild-type enzyme
K433A
-
102% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 95% of the mannose-phosphorylation of the wild-type enzyme
K457G
-
7.5% enzyme activity in comparison to wild-type enzyme
K457G
-
7.5% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 60% of total activity compared to 35% of the wild-type enzyme. 31% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158
K457R
-
45% enzyme activity in comparison to wild-type enzyme
K457R
-
45% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 60% of total activity compared to 35% of the wild-type enzyme. 33% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158
K457S
-
25% enzyme activity in comparison to wild-type enzyme
K457S
-
25% of the activity of wild-type enzyme when expressed in BHK cells. 50% of the mannose-phosphorylation of the wild-type enzyme. Mutation leads to an increase of enzyme activity in the medium to about 65% of total activity compared to 35% of the wild-type enzyme. 50% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158
K463Q
-
14% enzyme activity in comparison to wild-type enzyme
K463Q
-
14% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an decrease of enzyme activity in the medium to about 25% of total activity compared to 35% of the wild-type enzyme
K463R
-
39% enzyme activity in comparison to wild-type enzyme
K463R
-
39% of the activity of wild-type enzyme when expressed in BHK cells. 31% of the mannose-phosphorylation of the wild-type enzyme. Mutation leads to an decrease of enzyme activity in the medium to about 25% of total activity compared to 35% of the wild-type enzyme
N158Q/N350Q
-
43% enzyme activity in comparison to wild-type enzyme
N158Q/N350Q
-
43% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 25% of total activity compared to 75% of the wild-type enzyme
N350S
-
about 15% reduction of enzyme activity in comparison to wild-type enzyme in vitro
N350S
mutation contributes to enzyme activity reduction
N350S
-
about 15% reduction of enzyme activity in comparison to wild-type enzyme in vitro, mutation found in a patient with metachromatic leukodystrophy
R288H
-
about 40% reduction of enzyme activity in comparison to wild-type enzyme in vitro
R288H
-
about 40% reduction of enzyme activity in comparison to wild-type enzyme in vitro, mutation found in a patient with metachromatic leukodystrophy
R496H
-
about 15% reduction of enzyme activity in comparison to wild-type enzyme in vitro
R496H
-
about 15% reduction of enzyme activity in comparison to wild-type enzyme in vitro, mutation found in a patient with metachromatic leukodystrophy
additional information
-
R288H, N350S and R496H are sequence alterations found in a patient with metachromatic leukodystrophy. W124ter mutation, which leads to a truncated enzyme and the mutations E382Q and C500F are found in an other patient.
additional information
-
only substitution of Lys457 causes a reduction of phosphorylation to 33% and increases secretion of the mutant enzyme
additional information
-
R288H, N350S and R496H are sequence alterations found in a patient with metachromatic leukodystrophy. W124ter mutation, which leads to a truncated enzyme and the mutations E382Q and C500F are found in an other patient
additional information
study of disease-causing mutations, severe phenotype of this patient depends not only on the two disease-causing mutations, but also to some extent on the pseudodeficiency mutations
additional information
the frameshift mutations g.445_446dupG and g.2590_2591dupC are associated with metachromatic leukodystrophy and lead 0.3% or 10% of wild type ARSA activity, respectively
additional information
-
the frameshift mutations g.445_446dupG and g.2590_2591dupC are associated with metachromatic leukodystrophy and lead 0.3% or 10% of wild type ARSA activity, respectively
additional information
naturally occuring ARSA polymorphisms, overview
additional information
-
secretion and half-life of wild-type enzyme are reduced upon co-expression of defective P377L-pdASA
additional information
characterization of pathogenic variants c.98T > C, c.195delC, c.229G > C, c.545C > G, c.674A > G, c.852T > A, and c.1274A > G, which were found when sequencing a cohort of 31 German metachromatic leukodystrophy families. Upon expression in immortalized, human multipotent mesenchymal stromal cells prepared from a patient deficient in ARSA activity, the seven mutants show ARSA activity of less than 10% when compared with wild type
additional information
-
sperm from AS-A null mice show a significant delay in cumulus oocyte complex dispersion, compared with wild-type sperm
additional information
coating culture plates with recombinant mouse ArsA stimulates adhesion of human microvascular endothelial cells to the plate followed by the formation of cell protrusions as well as lamellipodia
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Homo sapiens
brenda
Boehringer, J.; Santer, R.; Schumacher, N.; Gieseke, F.; Cornils, K.; Pechan, M.; Kustermann-Kuhn, B.; Handgretinger, R.; Schoels, L.; Harzer, K.; Kraegeloh-Mann, I.; Mueller, I.
Enzymatic characterization of novel arylsulfatase A variants using human arylsulfatase A-deficient immortalized mesenchymal stromal cells
Hum. Mutat.
38
1511-1520
2017
Homo sapiens (P15289)
brenda
Issa, A.B.; Feki, F.K.; Jdila, M.B.; Khabou, B.; Rhouma, B.B.; Ammar-Keskes, L.; Triki, C.; Fakhfakh, F.
Clinical, molecular, and computational analysis showed a novel homozygous mutation among the substrate-binding site of ARSA protein in consanguineous family with late-infantile MLD
J. Mol. Neurosci.
66
17-25
2018
Homo sapiens (P15289)
brenda