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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
- urine
- steroid
- mucopolysaccharidosis
- sulfatide
- urinary
- asa
- leukocyte
- estrone
- glycosaminoglycans
- heparan
- urease
- cerebroside
- glucuronide
- aromatase
-
sulfotransferase
- demyelination
- estradiol
-
desulfation
- dehydroepiandrosterone
-
infantile
- dermatan
- beta-glucosidase
-
17beta-hydroxysteroid
-
mucopolysaccharide
- 4-sulfate
- pomatia
- hexosaminidase
- ichthyosis
- sulfamate
- galactosylceramide
- analysis
-
deconjugation
-
sanfilippo
- dysostosis
- 17beta-hsds
-
iduronate
-
hspgs
- alpha-l-iduronidase
-
saposins
-
chondrodysplasia
- tibolone
- mucolipidosis
- medicine
- galns
- synthesis
- punctata
- alpha-fucosidase
- morquio
-
loam
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
4-methylumbelliferyl sulfatase, ARS, ARS-A, ARS-B, ARSA, ARSB, ARSE, ARSK, ary 423, Aryl-sulfate sulphohydrolase, 
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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-fluoro-4-nitrophenyl sulfate + H2O
2-fluoro-4-nitrophenol + sulfate
-
-
-
?
2-hydroxy-4-nitrophenyl sulfate + H2O
2-hydroxy-4-nitrophenol + sulfate
-
-
-
-
?
2-methyl-4-nitrophenyl sulfate + H2O
2-methyl-4-nitrophenol + sulfate
-
-
-
-
?
3,4-dimethylphenyl sulfate + H2O
3,4-dimethylphenol + sulfate
-
-
-
?
3,4-dinitrophenyl sulfate + H2O
3,4-dinitrophenol + sulfate
-
-
-
?
3-fluoro-4-nitrophenyl sulfate + H2O
3-fluoro-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
-
-
-
-
?
epitestosterone 17-sulfate + H2O
epitestosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
etiocholanolone 3-sulfate + H2O
etiocholanolone + sulfate
reaction of EC 3.1.6.2
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate + H2O
N-benzyloxycarbonyl-L-Phe-L-Tyr + -sulfate
-
-
-
-
?
phloroglucinol monosulfate + H2O
phloroglucinol + sulfate
-
-
-
-
?
sulfated polysaccharide + H2O
polysaccharide + sulfate
-
-
-
?
testosterone 17-sulfate + H2O
testosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
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
-
-
-
-
?
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
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
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
-
-
-
?
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
-
-
-
?
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
-
-
?
androsterone 3-sulfate + H2O
androsterone + sulfate
reaction of EC 3.1.6.2
-
-
?
androsterone 3-sulfate + H2O
androsterone + sulfate
reaction of EC 3.1.6.2
-
-
?
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
-
-
-
-
?
dehydroepiandrosterone 3-sulfate + H2O
dehydroepiandrosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
dehydroepiandrosterone 3-sulfate + H2O
dehydroepiandrosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
epiandrosterone 3-sulfate + H2O
epiandrosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
epiandrosterone 3-sulfate + H2O
epiandrosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
estrone 3-sulfate + H2O
estrone + sulfate
reaction of EC 3.1.6.2
-
-
?
estrone 3-sulfate + H2O
estrone + sulfate
reaction of EC 3.1.6.2
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
the mechanism for S-O-bridge bond fission shifts, with decreasing leaving group ability, from charge compensation via Lewis acid interactions toward direct proton donation. The transition state for enzyme-catalyzed sulfate monoester hydrolysis has a significantly more associative character compared to the uncatalyzed reaction
-
-
?
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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
Ba2+
Ca2+
phosphate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
sulfate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
additional information
neither inhibitory nor activating: Ca2+, K+, Ba2+, Mg2+, Mn2+ and Sn2+
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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
Al3+
1 mM, less than 20% residual activity, both free and immobilized enzyme
Fe2+
1 mM, less than 20% residual activity, both free and immobilized enzyme
guanidine hydrochloride
1 mM, 69.5% of initial activity, mutant H260L
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
Triton X-100
1 mM, 15% residual activity, free enzyme, 35% residual activity, immobilized enzyme, respectively
Tween 80
1 mM, 10% residual activity, free enzyme, 60% residual activity, immobilized enzyme, respectively
2-mercaptoethanol
1 mM, 70% residual activity, both free and immobilized enzyme
2-mercaptoethanol
1 mM, 81% of initial activity, mutant H260L
Ag+
1 mM, less than 20% residual activity, both free and immobilized enzyme
Cd2+
1 mM, less than 20% residual activity, both free and immobilized enzyme
Cu2+
1 mM, less than 20% residual activity, both free and immobilized enzyme
dithiothreitol
1 mM, 69.8% of initial activity, mutant H260L
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
Fe3+
1 mM, less than 20% residual activity, both free and immobilized enzyme
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
PMSF
1 mM, 15% residual activity, free enzyme, 35% residual activity, immobilized enzyme, respectively
SDS
1 mM, 5% residual activity, free enzyme, 45% residual activity, immobilized enzyme, respectively
Zn2+
1 mM, less than 20% residual activity, both free and immobilized enzyme
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
-
additional information
neither inhibitory nor activating: Ca2+, K+, Ba2+, Mg2+, Mn2+ and Sn2+
-
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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
1.02
4-ethylphenyl sulfate
-
pH 7.0, temperature not specified in the publication
0.161
ferulic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
0.112
methylurolithin A sulfate
-
pH 7.0, temperature not specified in the publication
-
1.486
N-acetyltyramine sulfate
-
pH 7.0, temperature not specified in the publication
0.262
p-coumaric acid sulfate
-
pH 7.0, temperature not specified in the publication
0.131
resorcinol sulfate
-
pH 7.0, temperature not specified in the publication
0.341
vanillic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
0.085
2-hydroxy-5-nitrophenyl sulfate
-
in presence of 100 mM acetate and 100 mM sulfate
0.175
4-Methylumbelliferyl sulfate
-
pH 7.0, temperature not specified in the publication
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
0.0137
4-nitrophenyl sulfate
pH not specified in the publication, temperature not specified in the publication
0.66
4-nitrophenyl sulfate
mutant H260L, pH 7.5, 55°C
0.89
4-nitrophenyl sulfate
pH 7.5, 50°C, immobilized enzyme
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
7150
4-ethylphenyl sulfate
-
pH 7.0, temperature not specified in the publication
28600
4-Methylumbelliferyl sulfate
-
pH 7.0, temperature not specified in the publication
138
ferulic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
88500
methylurolithin A sulfate
-
pH 7.0, temperature not specified in the publication
-
1800
N-acetyltyramine sulfate
-
pH 7.0, temperature not specified in the publication
235
p-coumaric acid sulfate
-
pH 7.0, temperature not specified in the publication
1000
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase, at 45°C and pH 7.0
119
vanillic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
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
256.9
4-nitrophenyl sulfate
pH 7.5, 50°C, immobilized enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
164
4-Methylumbelliferyl sulfate
-
pH 7.0, temperature not specified in the publication
0.86
ferulic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
787
methylurolithin A sulfate
-
pH 7.0, temperature not specified in the publication
-
1.2
N-acetyltyramine sulfate
-
pH 7.0, temperature not specified in the publication
0.9
p-coumaric acid sulfate
-
pH 7.0, temperature not specified in the publication
0.35
vanillic acid 4-sulfate
-
pH 7.0, temperature not specified in the publication
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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
additional information
-
0.00006 and 0.00002 micromol/min/ml rennet of two calf rennet samples with p-nitrophenyl sulfate as substrate
additional information
-
0.00008 micromol/min/ml milk for pasteurized milk, p-nitrocatechol sulfate as substrate
additional information
-
0.00016 micromol/min/ml milk for raw milk, p-nitrocatechol sulfate as substrate
additional information
-
arylsulfatase activity not detectable in two calf rennet samples with p-nitrocatechol sulfate as substrate, activity is detectable with p-nitrophenyl sulfate
additional information
-
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
additional information
-
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
additional information
-
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
additional information
-
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
additional information
-
0.00014 micromol/min/ml milk for pasteurized milk, p-nitrocatechol sulfate as substrate
additional information
-
0.00067 micromol/min/ml milk for raw milk, p-nitrocatechol sulfate as substrate
additional information
-
not detectable in lamb rennet with p-nitrophenyl sulfate as substrate, but detectable with p-nitrocatechol sulfate as substrate
additional information
-
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
6.2
6.5
7.5
8.4
8.5
5.5
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate in acetic acid/sodium acetate buffer
6
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate in citric acid/sodium citrate 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 - 6
4 - 7
-
pH 4: about 15% of maximal activity, pH 7.0: about 55% of maximal activity
5 - 7
5 - 7.4
-
50% of maximal activity at pH 5.0 and at pH 7.4, hydrolysis of 4-nitrophenyl sulfate or 4-nitrocatecholsulfate
5.2 - 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
-
pH 7.5: about 30% of maximal activity, pH 10: about 90% of maximal activity, enzyme Es-2
7.5 - 10.2
-
pH 7.5: about 55% of maximal activity, pH 10.2: about 10% of maximal activity
4 - 6
-
pH 4: about 35% of maximal activity, pH 6.0: about 75% of maximal activity
5 - 7
-
pH 5.0: about 55% of maximal activity, pH 7.0: about 35% of maximal activity, hydrolysis of 4-nitrophenyl sulfate
5 - 7
-
pH 5.0: about 75% of maximal activity, pH 7.0: about 45% of maximal activity, hydrolysis of 4-nitrocatechol sulfate
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
40
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
10 - 60
-
10°C: about 35% of maximal activity, 60°C: about 30% of maximal activity
4 - 50
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
-
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
-
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
-
sulfatase mRNA expression levels in 13 malignant and nonmalignant tissue samples, 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
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
metabolism
-
in southwest China, soil arylsulfatase activity increases from cropland through to forest following post-agriculture succession, and is significantly lower in clasolite than in dolomite or limestone. Among 14 studied soil variables, soil pH, exchangeable calcium, organic carbon, clay and silt showed significant non-linear relationships with arylsulfatase activity. The activity of soil arylsulfatase is most controlled by soil pH and soil texture, but soil calcium and organic carbon only have indirect or spurious effects on arylsulfatase activity
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
physiological function
-
strain Kluyveromyces lactis DSM 70799 has no arylsulfatase activity, whereas the strain GG799 does. The only difference is a base substitution at position 415 resulting in an amino acid exchange from R139 in strain DSM 70799 to S139 in strain GG799. Amino acid position 139 is far away from the catalytic site of the arylsulfatase. The posttranslational modification of C56 to formylglycine is not found in the R139 variant. By contrast, the C56 residue of the S139 variant is modified. The inactive R139 variant exhibits a different structure regarding folding and packing compared to the active S139 variant
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
349000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
40000
45000
460000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
49000
63000
68000
70000
40000
-
the enzyme has the ability to complex to molecular masses of more than 300000, gel filtration