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Information on EC 3.1.6.1 - arylsulfatase
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3.1.6.1 arylsulfataseIUBMB Comments
A group of enzymes with rather similar specificities.
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Word Map
- 3.1.6.1
- lysosomal
-
metachromatic
- leukodystrophy
- beta-glucuronidase
- sulfatide
- mucopolysaccharidosis
- estrone
- leukocyte
-
sulfotransferase
- glycosaminoglycans
- demyelination
- estradiol
- aromatase
- urease
-
glucuronide
- cerebroside
-
heparan
-
infantile
- beta-glucosidase
-
desulfation
- dermatan
- dehydroepiandrosterone
- ichthyosis
-
mucopolysaccharide
-
hormone-dependent
- n-acetylgalactosamine
- hexosaminidase
- pomatia
-
17beta-hydroxysteroid
- 4-sulfate
-
a-deficient
-
hspgs
- tibolone
-
deconjugation
- dysostosis
- sulfamate
-
chondrodysplasia
- punctata
- medicine
- beta-hexosaminidase
- alpha-fucosidase
-
intralysosomal
- alpha-l-iduronidase
- analysis
- synthesis
-
iduronate
- morquio
- 17beta-hsds
- galns
-
sanfilippo
- mucolipidosis
-
saposins
- galactosylceramide
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
sulfatase, arylsulfatase a, arylsulphatase, arylsulfatase b, arylsulphatase a, estrogen sulfatase, ars-a, arylsulfatase e, arylsulfatase gene, arylsulfatase g, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methylumbelliferyl sulfatase
-
-
-
-
ARS
-
-
-
-
ARSA
ARSB
Aryl-sulfate sulphohydrolase
-
-
-
-
arylsulfatase
arylsulfatase A
arylsulfatase B
arylsulfatase Es-2
arylsulfatase G
arylsulfohydrolase
-
-
-
-
arylsulphatase
-
-
-
-
arylsulphatase A
AtsA
estrogen sulfatase
-
-
-
-
nitrocatechol sulfatase
-
-
-
-
p-nitrophenyl sulfatase
-
-
-
-
P70
-
the protein inhibits Na+,K+-ATPase activity and shows strong arylsulphatase A like activity
phenolsulfatase
-
-
-
-
phenylsulfatase
-
-
-
-
sulfatase
sulfatase, aryl-
-
-
-
-
arylsulfatase
-
-
-
-
sulfatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phenol sulfate + H2O = a phenol + sulfate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
aryl-sulfate sulfohydrolase
A group of enzymes with rather similar specificities.
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CAS REGISTRY NUMBER
COMMENTARY
9016-17-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chloro-4-nitrophenyl sulfate + H2O
sulfate + 2-chloro-4-nitrophenol
-
-
-
-
?
2-hydroxy-4-nitrophenyl sulfate + H2O
2-hydroxy-4-nitrophenol + sulfate
-
-
-
-
?
2-methyl-4-nitrophenyl sulfate + H2O
2-methyl-4-nitrophenol + sulfate
-
-
-
-
?
3-indoxyl sulfate + H2O
1H-indol-3-ol + sulfate
-
6.4% of the activity with 4-nitrophenyl sulfate
-
-
?
4-hydroxy-2-nitrophenyl sulfate + H2O
4-hydroxy-2-nitrophenol + sulfate
-
-
-
-
?
4-hydroxy-3-nitrophenyl sulfate + H2O
4-hydroxy-3-nitrophenol + sulfate
-
-
-
-
?
6-benzoyl-2-naphthyl sulfate + H2O
6-benzoyl-2-naphthol + sulfate
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate methyl ester + H2O
benzyloxycarbonyl-L-Phe-L-Tyr + methylsulfate
-
-
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
-
-
-
-
?
phloroglucinol monosulfate + H2O
phloroglucinol + sulfate
-
-
-
-
?
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
-
-
-
-
?
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
-
-
-
-
?
3-carboxyphenyl sulfate + H2O
3-carboxyphenol + sulfate
-
weak activity
-
-
?
3-carboxyphenyl sulfate + H2O
3-carboxyphenol + sulfate
-
weak activity
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
-
rather poor substrate
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
77% of the activity with 4-nitrophenyl sulfate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
J9QXV9
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
J9QXV9
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
the enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate. Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond. The rate-determining steps are different in the two reactions, i.e. nucleophile attack vs. nucleophile activation
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
J9QXV9
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
J9QXV9
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
the enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate. Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond. The rate-determining steps are different in the two reactions, i.e. nucleophile attack vs. nucleophile activation
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
?
agar + H2O
?
sulfate content of agar is diminished to 40% after a 12 h treatment
-
-
?
agar + H2O
?
sulfate content of agar is diminished to 40% after a 12 h treatment
-
-
?
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
-
-
-
-
?
additional information
?
-
-
no substrate: 5-bromo-4-chloro-3-indolyl sulfate, phenolphthalein disulfate, galactose 6-sulfate
-
-
-
additional information
?
-
-
enzyme might be of physiological significance in the deconjugation of the catecholamine sulfate isomers
-
-
-
additional information
?
-
activity is dependent on residue cysteine80, which undergoes conversion to formylglycine. No substrate: 4-methylumbelliferyl sulfate
-
-
-
additional information
?
-
-
enzyme is able to disperse the cumulus matrix of expanded cumulus oocyte complexes, this dispersion action is not associated with desulfation activity
-
-
-
additional information
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme might be of physiological significance in the deconjugation of the catecholamine sulfate isomers
-
-
-
additional information
?
-
-
enzyme is able to disperse the cumulus matrix of expanded cumulus oocyte complexes, this dispersion action is not associated with desulfation activity
-
-
-
additional information
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
phosphate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
sulfate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(alpha-acetonylbenzyl)-4-hydroxycoumarin
-
2.5 mM results in 50% reduced activity of arylsulfatase
IPTG
-
at concentrations from 50 micromolar up to 5000 micromolar of IPTG the activity decreases by more than 50%
N-benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate methyl ester
-
hydrolysis of 4-nitrophenyl sulfate
praziquantel
-
schistosomical drug, inhibitory to enzyme. No effect on immunological properties of enzyme
EDTA
-
0.1 mM EDTA 46.8% relative activity, 0.5 mM EDTA 39.6% relative activity and 1.0 mM EDTA 30.5% relative activity compared to the control
phosphate
-
acts as a strong, competitive ASG inhibitor, inhibition of ASG by phosphate is much stronger than by sulfate
PMSF
-
0.1 mM PMSF 92.7% relative activity, 0.5 mM PMSF 82.6% relative activity and 1.0 mM PMSF 73.5% relative activity compared to the control
additional information
-
SO42- and Ag+ ions have no effect on the enzyme activity
-
additional information
-
ASG is not inhibited by warfarin even at concentrations close to the solubility limit
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Commiphora extract
-
schistosomical drug, activating to enzyme. No effect on immunological properties of enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.085
2-hydroxy-5-nitrophenyl sulfate
-
in presence of 100 mM acetate and 100 mM sulfate
0.0291
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25°C
0.0752
4-nitrophenyl phosphate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C
0.00025
4-nitrophenyl sulfate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C
0.00029
4-nitrophenyl sulfate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25°C
0.0004
4-nitrophenyl sulfate
-
mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25°C
0.67
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase incubated at 45°C and at pH 7.0 in the presence of 10 mM sulfate
1.15
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase incubated at 45°C and at pH 7.0
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1000
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase, at 45°C and pH 7.0
0.0000095
4-nitrophenyl phosphate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C
0.023
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25°C
0.000061
4-nitrophenyl sulfate
-
mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25°C
0.0054
4-nitrophenyl sulfate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C
14.2
4-nitrophenyl sulfate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0292
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
468
-
7.1 mM p-nitrophenyl sulfate at 45°C and at pH 8.5, after Heparin-Sepharose column chromatography
additional information
additional information
-
0.00003 micromol/min/ml milk for raw milk with p-nitrophenyl sulfate as substrate; 0.00006 and 0.00002 micromol/min/ml rennet of two calf rennet samples with p-nitrophenyl sulfate as substrate; 0.00008 micromol/min/ml milk for pasteurized milk, p-nitrocatechol sulfate as substrate; 0.00016 micromol/min/ml milk for raw milk, p-nitrocatechol sulfate as substrate; arylsulfatase activity not detectable in two calf rennet samples with p-nitrocatechol sulfate as substrate, activity is detectable with p-nitrophenyl sulfate; no activity detectable in pasteurized milk with p-nitrophenyl sulfate as substrate
additional information
-
0.00011 micromol/min/ml rennet for kid rennet with p-nitrocatechol sulfate as substrate; 0.00017 micromol/min/ml rennet of kid rennet with p-nitrophenyl sulfate as substrate
additional information
-
0.0006 micromol/min/g wet cells of E. coli, at pH 7.0 with 4 mM methylumblliferyl sulfate; 0.0008 micromol/min/g wet cells of E. coli overexpressing a human alcohol sulfotransferase, at pH 7.0 with 4 mM methylumblliferyl sulfate
additional information
-
6 to 7-fold increase of activity compared to the negative control with the empty vector pCDL; incubation for 10 min of arylsulfatase at 50°C results in a decrease of activity by about 50%
additional information
-
0.00003 micromol/min/ml rennet for lamb rennet with p-nitrocatechol sulfate as substrate; 0.00014 micromol/min/ml milk for pasteurized milk, p-nitrocatechol sulfate as substrate; 0.00067 micromol/min/ml milk for raw milk, p-nitrocatechol sulfate as substrate; not detectable in lamb rennet with p-nitrophenyl sulfate as substrate, but detectable with p-nitrocatechol sulfate as substrate; not detectable in raw milk or pasteurized milk with p-nitrophenyl sulfate as substrate, but detectable with p-nitrocatechol sulfate as substrate
additional information
-
2.1 µmol/min/mL was measured at 50 mM p-nitrophenyl sulfate, pH 8.5 and 40°C, with 10 µM IPTG
additional information
-
0.0056 micromol/min/g wet cells of liver, at pH 7.0 with 4 mM methylumblliferyl sulfate
additional information
-
0.0008 micromol/min/g wet cells of liver, at pH 7.0 with 4 mM methylumblliferyl sulfate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
5 - 5.6
-
pH optimum gradually changes from pH 5.6 to 5.0 when the time of incubation is prolonged from 5 to 30-120 min
5.4
5.5
5.6
6 - 6.5
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate and 2-hydroxy-4-nitrophenyl sulfate
6
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate in citric acid/sodium citrate buffer
6.2
6.5
7.5
8.4
-
hydrolysis of 4-nitrophenyl sulfate, beta enzyme; hydrolysis of nitrocatechol sulfate, beta enzyme
8.5
5.5
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate in acetic acid/sodium acetate buffer
7
-
activity of purified arylsulfatase analysed at 40°C and at pH 4.5 to 10, p-nitrophenyl sulfate as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
-
pH 4: about 15% of maximal activity, pH 7.0: about 55% of maximal activity
4 - 6
-
about 45% maximal activity at pH 4 and pH 6, arylsulfatase A; pH 4: about 35% of maximal activity, pH 6.0: about 75% of maximal activity
5 - 7.4
-
50% of maximal activity at pH 5.0 and at pH 7.4, hydrolysis of 4-nitrophenyl sulfate or 4-nitrocatecholsulfate
5 - 7
-
pH 5.0: about 55% of maximal activity, pH 7.0: about 35% of maximal activity, hydrolysis of 4-nitrophenyl sulfate; pH 5.0: about 75% of maximal activity, pH 7.0: about 45% of maximal activity, hydrolysis of 4-nitrocatechol sulfate
5.2 - 7.9
-
pH 5.2: about 70% of maximal activity, pH 7.9: about 50% of maximal activity
6 - 8
pH 6.0: about 25% of maximal activity, pH 8.0: about 85% of maximal activity
7 - 10
7.4 - 10
-
pH 7.4: about 35% of maximal activity, 10.0: about 50% of maximal activity
7.5 - 10.2
-
pH 7.5: about 55% of maximal activity, pH 10.2: about 10% of maximal activity
7.5 - 10
-
pH 7.5: about 30% of maximal activity, pH 10: about 90% of maximal activity, enzyme Es-2
7 - 10
-
pH 7: about 40% of maximal activity, pH 10: about 60% of maximal activity, strain R-0827
7 - 10
-
pH 7: about 35% of maximal activity, pH 10: about 60% of maximal activity, strain SH 10-6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
45
additional information
Littorina kurila
-
50% loss in activity at 60°C compared to control condition of 37°C
45
-
purified arylsulfatase analysed at pH 7.0 and temperature between 10 to 80°C, p-nitrophenyl sulfate as substrate
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
10 - 60
-
10°C: about 35% of maximal activity, 60°C: about 30% of maximal activity
40 - 65
-
40°C: about 40% of maximal activity, 65°C: about 60% of maximal activity
60 - 90
60°C: about 60% of maximal activity, 90°C: about 30% of maximal activity
4 - 50
-
4°C: about 40% of maximal activity, 50°C: about 45% of maximal activity
4 - 50
-
4°C: about 40% of maximal activity, 50°C: about 25% of maximal activity, enzyme ES-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
marked derepression of enzyme in synthetic medium by addition of tyramine
-
-
brenda
strain A, strain KB, strain K, strain A 1-5, strain No. 35 and strain S4-15
-
-
brenda
-
-
-
brenda
two electrophoretically distinct enzyme forms: alpha and beta
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme expression is unaltered in cancer tissue compared to nonmalignant tissue
brenda
-
very low enzymic activity at 41 weeks of gestation, which reduce to a half at 42 weeks of gestation, while values of sulfatide concentrations increase
brenda
-
specific activity of enzyme remains low until testes reach a weight of approximately 1 g and then increases. Testes and epididymal regression induced by a short photoperiod increases enzyme activity in the testes and reduces activity in epididymides
brenda
-
primary epithelial cell, highest activity of galacose 6-sulfatase and aryl sulfatase B of all the cell lines tested
brenda
-
enzyme expression is unaltered in breast cancer tissue compared to nonmalignant tissue
brenda
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
brenda
-
primary myoepithelial cell, highest activity of steryl sulfatase and aryl sulfatase B of all the cell lines tested
brenda
-
localized at sperm head surface. Enzyme is able to disperse the cumulus matrix of expanded cumulus oocyte complexes, this dispersion action is not associated with desulfation activity
brenda
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
brenda
additional information
-
no significant changes in enzyme level upon feeding ethanol-containing Lieber-DeCarli liquid diet
brenda
-
no significant changes in enzyme level upon feeding ethanol-containing Lieber-DeCarli liquid diet
brenda
-
enzyme level decreases in animals receiving ethanol-containing Lieber-DeCarli liquid diet compared with control diet
brenda
-
In the sinusoidal endothelial cells, both surfaces of the luminal side and outside of sinusoid are positively stained
brenda
-
In the sinusoidal endothelial cells, both surfaces of the luminal side and outside of sinusoid are positively stained
brenda
-
raw milk or pasteurized milk incubated at 60°C for 30 min; raw milk or pasteurized milk which was incubated at 60°C for 30 min
brenda
-
; placental membrane, far from and close to internal uterine os
brenda
-
specific activity of enzyme is the highest in testis weighing from 20 to 200 mg, and then decreases as the weight of testis increases. Total enzyme activity shows a steady increase with the increasing weight of testes. Testes and epididymal regression induced by a short photoperiod increases enzyme activity in the testes and reduces activity in epididymides
brenda
additional information
-
sulfatase mRNA expression levels in 13 malignant and nonmalignant tissue samples, overview
brenda
additional information
-
activity of arylsulphatase A decreases in the cord, in membranes far from the internal uterine os, in membranes close to the internal uterine os and in the placenta of healthy gravidas at term pregnancy, following spontaneous birth, overview
brenda
additional information
mRNA expression is found in all tissues tested
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
32% of arylsulfatase acivity is intracellular
brenda
-
32% of arylsulfatase acivity is intracellular
-
brenda
protein carries mannose 6-phosphate, indicating lysosomal sorting
brenda
63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association. Lysosomal transport of arylsulfatase G in the liver is independent of mannose 6-phosphate, sortilin, and Limp2. Mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification
brenda
-
inside membrane-bound cytoplasmic vesicles distributed throughout the cell body
brenda
J9QXV9
99% of arylsulfatase activity is membrane-associated
brenda
-
99% of arylsulfatase activity is membrane-associated
-
brenda
63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association
brenda
99% of arylsulfatase activity is membrane-associated
brenda
-
99% of arylsulfatase activity is membrane-associated
-
brenda
68% of arylsulfatase acivity is membrane-associated
brenda
-
68% of arylsulfatase acivity is membrane-associated
-
brenda
additional information
-
immunohistochemic localization analysis, overview. ARSA and ARSB are also colocalized with heparan sulfate proteoglycan
-
brenda
additional information
-
immunohistochemic localization analysis, overview. ARSA and ARSB are also colocalized with heparan sulfate proteoglycan
-
brenda
additional information
-
enzyme is not secreted by epimastigote or trypomastigote form and not detected in epimastigote reservosome
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
metachromatic leukodystrophy, MLD, is a lethal neurodegenerative disease caused by a deficiency in the lysosomal arylsulfatase A enzyme leading to the accumulation of sulfatides in glial and neuronal cells
malfunction
-
metachromatic leukodystrophy, MLD, is an autosomal recessive, lysosomal storage disease caused by a deficiency of the enzyme arylsulfatase A, ARSA
physiological function
-
arylsulphatase A is a lysosomal enzyme that catabolizes sulphatides, it is likely to be under hormonal control, in particular, by estradiol and progesterone
physiological function
a one-time injection of human arylsufatase B into injured mouse spinal cord eliminates immunoreactivity for chondroitin sulfates within five days, and up to 9 weeks after injury. After a moderate spinal cord injury, locomotor recovery assessed by the Basso Mouse Scale in arylsulfatase B treated mice improves, compared to the buffer-treated control group, at 6 weeks after injection. After a severe spinal cord injury, mice injected with equivalent units of arylsulfatase B or bacterial chondroitinase ABC improve similarly and both groups achieve significantly more locomotor recovery than the buffer-treated control mice. Serotonin and tyrosine hydroxylase immunoreactive axons are more extensively present in mouse spinal cords treated with arylsulfatase B and chondroitinase ABC, and the immunoreactive axons penetrate further beyond the injury site than in control mice
Show AA Sequence and Transmembrane Helices (3824 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
45000
49000
63000
68000
70000
100000
349000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
460000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
40000
-
the enzyme has the ability to complex to molecular masses of more than 300000, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
enzyme has a specific affinity for chondroitin sulfate B, a component of the cumulus matrix proteoglycan network
?
x * 68000, SDS-PAGE of recombinant glycoprotein, cellular form; x * 70000, SDS-PAGE of recombinant glycoprotein, secreted form
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
-
formylglycine is generated by posttranslational modification of a conserved cysteine residue. Cysteine is also converted to formylglycine when the gene is expressed in Escherichia coli. Substituting the relevant cysteine by a serine codon in the gene of Pseudomonas aeruginosa leads to expression of inactive sulfatase protein, lacking the formylglycine. The machinery catalyzing the modification of the Pseudomonas sulfatase in E. coli therefore accepts cysteine but not serine as a modification substrate
additional information
presence of a disulfide bridge between the processed 18-kDa fragment and another smaller polypeptide, probably involving residue Cys195 of the 10-kDa chain
glycoprotein
-
ASG is a glycoprotein that binds specifically to mannose 6-phosphate receptors, the activity of arylsulfatase G depends on the Cys84 residue that is predicted to be posttranslationally converted to the critical active site Calpha-formylglycine
glycoprotein
when expressed in human cells, isoform ArsK is detected as a 68-kDa glycoprotein carrying at least four N-glycans of both the complex and high-mannose type. Protein carries mannose 6-phosphate, indicating lysosomal sorting
glycoprotein
-
lowering pH and increasing glycosylation reduces the flexibility of the enzyme. At acidic pH, the glycosylated enzyme presents a higher secondary conformational stability when compared to its nonglycosylated counterpart
proteolytic modification
-
the enzyme is synthesized as a higher molecular mass precursor
proteolytic modification
63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association. Proteases participating in the processing are cathepsins B and L. Proteolytic processing is dispensable for hydrolytic sulfatase activity in vitro
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystals of arylsulfatase are obtained at a pH of 6.3 by hanging drop vapour diffusion method. The three-dimensional structure is determined to 1.3 A resolution in the space group C2. The asymmetric unit contains two monomers
-
full quantum chemical study performed at the density functional level, based on PDB entry 1HDH. The enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate.Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C80A
about 20% of wild-type activity at neutral pH, about 5% of wild-type activity at pH optimum
G137A
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
I40S
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
N350S
-
mutant exhibits a consistent degree of unfolding, which may be related to its in vitro reduced stability
P578S
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
T409M
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
W124G
-
naturally occurring missense mutation causing ARSA deficiency, isolated from two Tunisian patients with late infantile metachromatic leukodystrophy, MLD
N497Q
mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification
additional information
additional information
-
intracerebral injection of a serotype 5 adeno-associated vector, AAV2-5, encoding human ARSA in ARSA-deficient mice corrects the biochemical, neuropathological and behavioral abnormalities. Injection in the right hemisphere and into three selected areas of the centrum semiovale white matter, or in the deep gray matter nuclei, caudate nucleus, putamen, thalamus, of six non-human primates, Macaca fascicularis, to evaluate vector distribution, as well as expression and activity of human ARSA, overview. ARSA enzyme is expressed in multiple interconnected brain areas and ARSA activity is increased by 12-38% in a brain volume that corresponded to 50–65% of injected hemisphere
additional information
-
sperm of enzyme deficient mice shows a significant delay in dispoersion of expanded cumulus oocyte complexes. Within 1 h of sperm-cumulus oocyte complex co-incubation, the size of cumulus oocyte complexes incubated with enzyme deficient sperm is 65% of its original dimension, whereas that of cumulus oocyte complexes inseminated with wild-type sperm is only 17%
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
below pH 4 in presence of 1% SDS arylsulfatase A is irreversibly converted into inactive subunits
135529
8 - 9.5
additional information
-
lowering pH and increasing glycosylation reduces the flexibility of the enzyme. At acidic pH, the glycosylated enzyme presents a higher secondary conformational stability when compared to its nonglycosylated counterpart
730069
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
60
60
-
rapidly inactivated at alkaline and acid pH, more thermostable at pH 6.5-7.0
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
several cycles of freezing and thawing cause a marked reduction of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
3°C, 0.1 M sodium phosphate buffer, 14 days, 25% loss of activity
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose anion-exchange and Heparin-Sepharose CL 6B affinity chromatography, all steps at 4°C
-
gel filtration on a Sepharose CL 6B column under elution with 0.025 M acetate buffer, pH 5.4
Littorina kurila
-
partial
retroviral expressed enzyme purified with ion-exchange DEAE-cellulose chromatography followed by immuno-affinity purification using a polyclonal antibody against arylsulfatase A sequence
-
use of solid phase extraction on a polymeric resin for purification without affecting the enzyme activity
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
ARSA, cloning of the coding sequence of the human ARSA cDNA tagged with HA epitope in C-terminus into viral serotype 5 adeno-associated vector, AAV2-5
-
ARSA, DNA and amino acid sequence determination and analysis of wild-type and mutant
-
astA gene from Pseudoalteromonas carrageenovora genome is subcloned into pHCEIA vector employing the hyper constitutive expression promoter from the D-amino acid aminotransferase gene of Geobacillus toebii. When the cell is cultured on fermentor containing MaxyBroth-HD medium with 1% glycerol, the enzyme activity reaches 12.8 micromol/min/mL. On MaxyBroth-HD medium with 2% glycerol, the cell shows 2.7fold higher arylsulfatase expression than that with 1% glycerol. The fed-batch cultivation employing MaxyBroth-HD medium and additional feeding of glycerol gave about 143 micromol/min/mL of arylsulfatase at 20 h, which corresponds to 4fold higher enzyme activity than that of 2% glycerol batch culture
-
expression in active form in a sulfatase-deficient strain of Pseudomonas aeruginosa, thereby restoring growth on aromatic sulfates as sole sulfur source, and in Escherichia coli.Cysteine is also converted to formylglycine in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
J9QXV9
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
-
-
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
-
-
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
-
-
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
J9QXV9
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
-
-
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
-
-
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
synthesis
analysis
-
cytochemical localization of enzyme in cytoplasmic vesicles as a specific detection method for lysosomes
analysis
-
distinction of lysosomes and reservosomes by cytochemical localization of enzyme in epimastigote and trypomastigote
medicine
-
use of immobilized and column-packed enzyme is an efficient alternative for the cleavage of urinary conjugates in clinical toxicology
medicine
-
the enzyme can be accepted as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy
medicine
-
leukocytes of patients with cerebral palsy show lower enzyme activity as compared to control. Km value for 4-nitrocatechol sulfate in patients' leukocytes is about 0.26 mM, in control 0.21 mM, whereas Vmax value in patients reaches only 58% of healthy control. All investigated patients reveal presence of the most common mutations associated with enzyme pseudodeficiency
medicine
-
very low enzymic activity in deciduum of women at 41 weeks of gestation, which reduce to a half at 42 weeks of gestation, while values of sulfatide concentrations increase
medicine
-
potential benefits of ARSA brain gene therapy in patients with metachromatic leukodystrophy, MLD
medicine
-
assay for the diagnosis of metachromatic leukodystrophy. Determination of arylsulfatase A activity toward the natural substrate, galactosyl-3-sulfate ceramide or sulfatide, is performed using neat sulfatide without chemical modification. The hydrolyzed sulfatide is monitored upon inclusion of the colorimetric reagent Azure A. Within a clinical context, the method definitely discriminates between healthy subject samples and metachromatic leukodystrophy patient samples
medicine
a one-time injection of human arylsufatase B into injured mouse spinal cord eliminates immunoreactivity for chondroitin sulfates within five days, and up to 9 weeks after injury. After a moderate spinal cord injury, locomotor recovery assessed by the Basso Mouse Scale in arylsulfatase B treated mice improves, compared to the buffer-treated control group, at 6 weeks after injection. After a severe spinal cord injury, mice injected with equivalent units of arylsulfatase B or bacterial chondroitinase ABC improve similarly and both groups achieve significantly more locomotor recovery than the buffer-treated control mice. Serotonin and tyrosine hydroxylase immunoreactive axons are more extensively present in mouse spinal cords treated with arylsulfatase B and chondroitinase ABC, and the immunoreactive axons penetrate further beyond the injury site than in control mice
medicine
-
the enzyme can be accepted as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy
-
synthesis
-
purification method for removing phytoestrogens and related compounds without affecting the enzyme activity. Use of solid phase extraction on a polymeric resin for purification
synthesis
the enzyme could be useful for producing a low sulfated agar and electrophoretic grade agarose
synthesis
-
the enzyme could be useful for producing a low sulfated agar and electrophoretic grade agarose
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toennes, S.W.; Maurer, H.H.
Efficient cleavage of conjugates of drugs or poisons by immobilized beta-glucuronidase and arylsulfatase in columns
Clin. Chem.
45
2173-2182
1999
Helix pomatia
brenda
Sampson, E.J.; Vergara, E.V.; Fedor, J.M.; Funk, M.O.; Benkovic, S.J.
On the physical properties and mechanism of action of arylsulfate sulfohydrolase II from Aspergillus oryzae
Arch. Biochem. Biophys.
169
372-383
1975
Aspergillus oryzae
brenda
Rasburn, M.; Wynn, C.H.
Purification and properties of an isoenzyme of arylsulphatase from Aspergillus oryzae
Biochim. Biophys. Acta
293
191-196
1973
Aspergillus oryzae
brenda
Delisle, G.J.; Milazzo, F.H.
Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa
Can. J. Microbiol.
18
561-568
1972
Pseudomonas aeruginosa
brenda
Lien, T.; Schreiner, O.
Purification of a derepressible arylsulfatase from Chlamydomonas reinhardtii. Properties of the enzyme in intact cells and in purified state
Biochim. Biophys. Acta
384
168-179
1975
Chlamydomonas reinhardtii
brenda
Okamura, H.; Yamada, T.; Murooka, Y.; Harada, T.
Purification and properties of arylsulfatase of Klebsiella aerogenes. Identity of the enzymes formed by non-repressed and de-repressed synthesis
Agric. Biol. Chem.
40
2071-2076
1976
Klebsiella aerogenes, Klebsiella aerogenes W70
-
brenda
De Hostos, E.L.; Togasaki, R.K.; Grossman, A.
Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii
J. Cell Biol.
106
29-37
1988
Chlamydomonas reinhardtii
brenda
Ueki, T.; Sawada, Y.; Fukagawa, Y.; Oki, T.
Arylsulfatase from Streptomyces griseorubiginosus S980-14
Biosci. Biotechnol. Biochem.
59
1062-1068
1995
Streptomyces griseorubiginosus, Streptomyces griseorubiginosus S980-14
brenda
Murooka, Y.; Yim, M.H.; Harada, T.
Formation and purification of Serratia marcescens arylsulfatase
Appl. Environ. Microbiol.
39
812-817
1980
Serratia marcescens
brenda
Sakurai, Y.; Isobe, K.; Shiota, H.
Partial purification and some properties of an alkaline arylsulfatase produced by Aspergillus fungi.
Agric. Biol. Chem.
44
1-7
1980
Aspergillus awamori, Aspergillus inuii, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus phoenicis R-0638, Aspergillus sojae, Aspergillus usamii, Aspergillus usamii R-1031
brenda
Roy, A.B.
Sulfatases from Helix pomatia
Methods Enzymol.
143
361-366
1987
Helix pomatia
brenda
Farooqui, A.A.; Hanson, W.L.
Comparison of arylsulphatases from Eimeria tenella (parasite) and chicken caecum (host)
Biochem. J.
242
97-102
1987
Eimeria tenella, Gallus gallus
brenda
Collett, R.A.
Arylsulphatase activity in liver and gastrointestinal tract of sheep
Biochem. Soc. Trans.
8
343-344
1980
Ovis aries
brenda
Moriya, T.; Hoshi, M.
Characterization and partial purification of arylsulfatase from the seminal plasma of the sea urchin, Strongylocentrotus intermedius
Arch. Biochem. Biophys.
201
216-223
1980
Strongylocentrotus intermedius
brenda
Clark, A.G.; Jowett, D.A.
Purification and properties of an arylsulphatase from the digestive gland of Haliotis iris
Comp. Biochem. Physiol. B
89
409-417
1988
Haliotis iris
-
brenda
Sasaki, H.; Akasaka, K.; Shimada, H.; Shiroya, T.
Purification and characterization of arylsulfatase from sea urchin (Hemicentrotus pulcherrimus) embryos
Comp. Biochem. Physiol. B
88
147-152
1987
Hemicentrotus pulcherrimus
-
brenda
Droba, M.
Comparative studies on arylsulphatases from fowl testes and seminal plasma
Folia Biol. (Krakow)
34
55-72
1986
Gallus gallus
brenda
Droba, M.; Droba, B.
Further studies on arylsulphatase activity from fowl seminal plasma
Folia Biol. (Krakow)
31
107-117
1983
Gallus gallus
brenda
Shapira, E.; Nadler, H.L.
Purification and some properties of soluble human liver arylsulfatases
Arch. Biochem. Biophys.
170
179-187
1975
Homo sapiens
brenda
Knoess, W.; Glombitza, K.W.
A phenylsulphatase from the marine brown alga Cystoseira tamariscifolia
Phytochemistry
32
1119-1123
1993
Cystoseira tamariscifolia
-
brenda
Beil, S.; Kehrli, H.; James, P.; Staudenmann, W.; Cook, A.M.; Leisinger, T.; Kertesz, M.A.
Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA)
Eur. J. Biochem.
229
385-294
1995
Pseudomonas aeruginosa
brenda
Van der Pal, R.H.M.; Klein, W.; van Golde, L.M.G.; Lopes-Cardozo, M.