Information on EC 3.1.6.1 - arylsulfatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.6.1
-
RECOMMENDED NAME
GeneOntology No.
arylsulfatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phenol sulfate + H2O = a phenol + sulfate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sphingolipid metabolism
-
-
Steroid hormone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
aryl-sulfate sulfohydrolase
A group of enzymes with rather similar specificities.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4-methylumbelliferyl sulfatase
-
-
-
-
ARS
-
-
-
-
ARS-A
-
-
ARS-B
-
-
ARSA
P15289
-
ARSB
P15848
-
ARSE
-
-
ARSK
Q6UWY0
-
Aryl-sulfate sulphohydrolase
-
-
-
-
arylsufatase B
P15848
-
arylsulfatase
-
-
-
-
arylsulfatase
-
-
arylsulfatase
-
-
arylsulfatase
Escherichia coli BL-21
-
-
-
arylsulfatase
-
-
arylsulfatase
-
-
arylsulfatase
Littorina kurila
-
-
arylsulfatase
-
-
arylsulfatase
-
-
arylsulfatase
-
-
arylsulfatase
-
-
arylsulfatase A
-
-
arylsulfatase A
-
-
arylsulfatase B
-
-
arylsulfatase B
-
-
arylsulfatase E
-
-
arylsulfatase Es-2
-
-
arylsulfatase Es-2
Streptomyces sp. T109-3
-
-
-
arylsulfatase G
-
-
arylsulfatase G
Q3TYD4
-
arylsulfatase gene
-
-
arylsulfatase III
-
-
arylsulfatase K
Q6UWY0
-
arylsulfatase type VI
-
-
arylsulfate sulfohydrolase II
-
-
arylsulfohydrolase
-
-
-
-
arylsulphatase
-
-
-
-
arylsulphatase A
-
-
arylsulphatase A
-
-
AS-A
-
-
estrogen sulfatase
-
-
-
-
KIAA1001
-
-
nitrocatechol sulfatase
-
-
-
-
p-nitrophenyl sulfatase
-
-
-
-
P70
-
the protein inhibits Na+,K+-ATPase activity and shows strong arylsulphatase A like activity
phenolsulfatase
-
-
-
-
phenylsulfatase
-
-
-
-
sulfatase
-
-
-
-
sulfatase
-
-
sulfatase, aryl-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9016-17-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain R-0827 and strain R-3523
-
-
Manually annotated by BRENDA team
strain R-3631 and strain R-1210
-
-
Manually annotated by BRENDA team
var. fermentarious
-
-
Manually annotated by BRENDA team
strain A, strain KB, strain K, strain A 1-5, strain No. 35 and strain S4-15
-
-
Manually annotated by BRENDA team
strain R-0638
-
-
Manually annotated by BRENDA team
Aspergillus phoenicis R-0638
strain R-0638
-
-
Manually annotated by BRENDA team
strain SH 10-1, strain SH 10-3, strain SH 21 and strain SH 10-6
-
-
Manually annotated by BRENDA team
strain R-1031
-
-
Manually annotated by BRENDA team
Aspergillus usamii R-1031
strain R-1031
-
-
Manually annotated by BRENDA team
type I arylsulfatase
-
-
Manually annotated by BRENDA team
marked derepression of enzyme in synthetic medium by addition of tyramine
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes W70
strain W70
-
-
Manually annotated by BRENDA team
BL-21 strain
-
-
Manually annotated by BRENDA team
Escherichia coli BL-21
BL-21 strain
-
-
Manually annotated by BRENDA team
bifunctional beta-glucuronidase/aryl sulfatase
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
patients with cerebral palsy
-
-
Manually annotated by BRENDA team
women at 41 and 42 weeks of gestation
-
-
Manually annotated by BRENDA team
Littorina kurila
-
-
-
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
isoform arylsulfatase B, in liver of Schistosoma-infected mouse
-
-
Manually annotated by BRENDA team
male ICR mice and Swiss mice
-
-
Manually annotated by BRENDA team
two electrophoretically distinct enzyme forms: alpha and beta
-
-
Manually annotated by BRENDA team
male adult Wistar rats
-
-
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
strain S980-14, arylsulfatase Es-1
-
-
Manually annotated by BRENDA team
Streptomyces griseorubiginosus S980-14
strain S980-14, arylsulfatase Es-1
-
-
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
strain T109-3, arylsulfatase Es-2
-
-
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
Streptomyces sp. T109-3
strain T109-3, arylsulfatase Es-2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P15848
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
show the reaction diagram
-
-
-
-
?
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
show the reaction diagram
-
-
-
-
?
2-carboxyphenyl sulfate + H2O
2-carboxyphenol + sulfate
show the reaction diagram
-
-
-
-
?
2-chloro-4-nitrophenyl sulfate + H2O
sulfate + 2-chloro-4-nitrophenol
show the reaction diagram
-
-
-
-
?
2-hydroxy-4-nitrophenyl sulfate + H2O
2-hydroxy-4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-methyl-4-nitrophenyl sulfate + H2O
2-methyl-4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-nitrophenyl sulfate + H2O
2-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-nitrophenyl sulfate + H2O
2-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-nitrophenyl sulfate + H2O
2-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
2-nitrophenyl sulfate + H2O
2-nitrophenol + sulfate
show the reaction diagram
Enterobacter aerogenes W70
-
-
-
-
?
3-carboxyphenyl sulfate + H2O
3-carboxyphenol + sulfate
show the reaction diagram
Enterobacter aerogenes, Enterobacter aerogenes W70
-
weak activity
-
-
?
3-indoxyl sulfate + H2O
1H-indol-3-ol + sulfate
show the reaction diagram
-
6.4% of the activity with 4-nitrophenyl sulfate
-
-
?
3-nitrophenyl sulfate + H2O
3-nitrophenol + sulfate
show the reaction diagram
Enterobacter aerogenes, Enterobacter aerogenes W70
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
show the reaction diagram
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
show the reaction diagram
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
show the reaction diagram
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
show the reaction diagram
Streptomyces griseorubiginosus S980-14
-
-
-
-
?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
show the reaction diagram
Streptomyces sp. T109-3
-
-
-
-
?
4-hydroxy-2-nitrophenyl sulfate + H2O
4-hydroxy-2-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-hydroxy-3-nitrophenyl sulfate + H2O
4-hydroxy-3-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
show the reaction diagram
Streptomyces griseorubiginosus, Streptomyces griseorubiginosus S980-14
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
show the reaction diagram
Streptomyces sp. T109-3
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
-
rather poor substrate
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
Escherichia coli BL-21
-
-
-
-
?
4-methylumbelliferylsulfate + H2O
4-methylumbelliferol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
-
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
Q6UWY0
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
best substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
-
77% of the activity with 4-nitrophenyl sulfate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
J9QRU6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
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
show the reaction diagram
J9QWA6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
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
show the reaction diagram
Enterobacter aerogenes W70
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
Streptomyces griseorubiginosus S980-14
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
Streptomyces sp. T109-3
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
J9QRU6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
show the reaction diagram
J9QWA6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
-
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
Q6UWY0
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
J9QRU6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
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
show the reaction diagram
J9QWA6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
Enterobacter aerogenes W70
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
Streptomyces griseorubiginosus S980-14
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
Streptomyces sp. T109-3
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
J9QRU6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
J9QWA6
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?
6-benzoyl-2-naphthyl sulfate + H2O
6-benzoyl-2-naphthol + sulfate
show the reaction diagram
-
-
-
-
?
agar + H2O
?
show the reaction diagram
-
-
-
-
?
androsterone sulfate + H2O
androsterone + sulfate
show the reaction diagram
-
-
-
-
?
apigenin-7,4'-disulfate + H2O
sulfate + ?
show the reaction diagram
-
-
-
-
?
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
show the reaction diagram
-
-
-
-
-
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
show the reaction diagram
-
-
-
-
?
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
show the reaction diagram
-
-
-
-
?
ascorbic acid 2-sulfate + H2O
ascorbic acid + sulfate
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate methyl ester + H2O
benzyloxycarbonyl-L-Phe-L-Tyr + methylsulfate
show the reaction diagram
-
-
-
-
?
cerebroside 3-sulfate + H2O
cerebroside + sulfate
show the reaction diagram
-
-
-
-
?
cerebroside 3-sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
chondroitin sulfate C + H2O
chondroitin + sulfate
show the reaction diagram
-
-
-
-
?
chondroitin sulfate C + H2O
chondroitin + sulfate
show the reaction diagram
-
-
-
-
?
chondroitin sulfate C + H2O
chondroitin + sulfate
show the reaction diagram
Streptomyces sp. T109-3
-
-
-
-
?
dopamine 3-sulfate + H2O
dopamine + sulfate
show the reaction diagram
-
-
-
-
-
dopamine 4-sulfate + H2O
dopamine + sulfate
show the reaction diagram
-
-
-
-
-
epinephrine 3-sulfate + H2O
epinephrine + sulfate
show the reaction diagram
-
-
-
-
-
epinephrine 4-sulfate + H2O
epinephrine + sulfate
show the reaction diagram
-
-
-
-
-
estrone 3-sulfate + H2O
sulfate + estrone
show the reaction diagram
-
-
-
-
?
estrone 3-sulfate + H2O
sulfate + estrone
show the reaction diagram
Streptomyces griseorubiginosus, Streptomyces griseorubiginosus S980-14
-
-
-
-
?
etoposide 4'-sulfate + H2O
etoposide + sulfate
show the reaction diagram
-
-
-
-
?
etoposide 4'-sulfate + H2O
etoposide + sulfate
show the reaction diagram
-
-
-
-
?
hydroquinone sulfate + H2O
hydroquinone + sulfate
show the reaction diagram
-
-
-
-
?
indoxyl sulfate + H2O
indoxol + sulfate
show the reaction diagram
-
weak activity
-
-
?
nitrocatechol sulfate + H2O
nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
nordopamine 3-sulfate + H2O
nordopamine + sulfate
show the reaction diagram
-
-
-
-
-
norepinephrine 3-sulfate + H2O
norepinephrine + sulfate
show the reaction diagram
-
-
-
-
-
norepinephrine 4-sulfate + H2O
norepinephrine + sulfate
show the reaction diagram
-
-
-
-
-
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
Littorina kurila
-
-
-
-
?
phenyl sulfate + H2O
phenol + sulfate
show the reaction diagram
-
-
-
-
?
phenyl sulfate + H2O
phenol + sulfate
show the reaction diagram
-
weak activity
-
-
?
phloroglucinol monosulfate + H2O
phloroglucinol + sulfate
show the reaction diagram
-
-
-
-
?
Tyr-O-sulfate + H2O
Tyr + sulfate
show the reaction diagram
-
weak activity
-
-
?
tyramine-O-sulfate + H2O
tyramine + sulfate
show the reaction diagram
-
weak activity
-
-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme might be of physiological significance in the deconjugation of the catecholamine sulfate isomers
-
-
-
additional information
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
-
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
?
-
-
no substrate: 5-bromo-4-chloro-3-indolyl sulfate, phenolphthalein disulfate, galactose 6-sulfate
-
-
-
additional information
?
-
-
ASG does not undergo lysosomal processing
-
-
-
additional information
?
-
Q6UWY0
activity is dependent on residue cysteine80, which undergoes conversion to formylglycine. No substrate: 4-methylumbelliferyl sulfate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
agar + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme might be of physiological significance in the deconjugation of the catecholamine sulfate isomers
-
-
-
additional information
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
-
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
?
-
-
ASG does not undergo lysosomal processing
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
can partially replace Ca2+
Ca2+
-
required
Mg2+
-
can partially replace Ca2+
NH4+
-
25 mM, 60% activation
phosphate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
Sr2+
-
can partially replace Ca2+
sulfate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
-
1,10-phenanthroline
-
-
1,2,3-benzoxathiazine 2,2-dioxide
-
irreversible
1,3-phenanthroline
-
-
2-(difluoromethyl)phenyl hydrogen sulfate
-
competitive
2-hydroxy-4-methyl-5-nitrophenyl sulfate
-
substrate inhibition
2-mercaptoethanol
-
-
3,4-dihydro-1,2,3-benzoxathiazine 2,2-dioxide
-
irreversible
3-(alpha-acetonylbenzyl)-4-hydroxycoumarin
-
2.5 mM results in 50% reduced activity of arylsulfatase
3H-1,2,3-benzoxathiazole 2,2-dioxide
-
irreversible
4-(difluoromethyl)phenyl hydrogen sulfate
-
competitive
4-nitrophenyl phosphate
-
hydrolysis of 4-nitrophenyl sulfate
4-nitrophenyl phosphate
-
-
4-nitrophenyl sulfate
-
substrate inhibition
4-nitrophenyl sulfate
-
substrate inhibition above 12 mM
5-sulfosalicylic acid
-
strong
AgNO3
-
0.2 mM, 20-30% inhibition
citrate
-
-
CN-
-
20 mM NaCN
CN-
-
no inhibition
CN-
-
weak inhibitor
dithiothreitol
-
-
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
Estrone 3-sulfate
-
-
heparin
-
-
Hg2+
-
HgCl2
hydroxylamine
-
-
hydroxylamine
-
-
imidazole
-
-
iodoacetate
-
-
iodoacetic acid
-
10 mM, 48% residual activity
IPTG
-
at concentrations from 50 micromolar up to 5000 micromolar of IPTG the activity decreases by more than 50%
K2HPO4
-
5 mM, 97-98% inhibition
KCN
-
10 mM, 23% residual activity
N-benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate methyl ester
-
hydrolysis of 4-nitrophenyl sulfate
Na2B4O7
-
10 mM, 12% residual activity
Na3PO4
-
competitive
NaCl
-
125 mM, 20-30% inhibition
Octopamine
-
-
p-(amidinophenyl)methanesulfonyl fluoride
-
-
p-(amidinophenyl)methanesulfonyl fluoride HCl
-
-
Phenolphthalein disulfate
-
hydrolysis of 4-nitrophenyl sulfate
phenyl sulfamate
-
irreversible
phosphate
-
acts as a strong, competitive ASG inhibitor, inhibition of ASG by phosphate is much stronger than by sulfate
phosphate
Q6UWY0
-
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
PO43-
-
no inhibition
PO43-
-
no inhibition
PO43-
-
potent inhibitor
praziquantel
-
schistosomical drug, inhibitory to enzyme. No effect on immunological properties of enzyme
SO32-
-
potent inhibitor
SO42-
-
competitive
SO42-
-
no inhibition
SO42-
-
no inhibition
SO42-
-
FeSO4
SO42-
-
FeSO4
SO42-
-
weak
SO42-
-
Na2SO4
SO42-
-
competitive; Na2SO4
SO42-
-
12.5 mM K2SO4, 80-85% inhibition
SO42-
-
K2SO4; MgSO4
SO42-
-
K2SO4
sodium dodecyl sulfonate
-
-
sodium dodecylsulfate
-
1 mM, 4% residual activity
sodium phenylmethane sulfonate
-
-
tyramine
-
10 mM, 14% residual activity
Warfarin
-
-
Zn2+
-
ZnCl2
ZnCl2
-
10 mM, 10% residual activity
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Commiphora extract
-
schistosomical drug, activating to enzyme. No effect on immunological properties of enzyme
-
EDTA
-
10 mM, 114% of initial activity
imidazole
-
strongly increases activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.181
2-hydroxy-4-nitrophenyl sulfate
-
in presence of 100 mM acetate
0.043
2-hydroxy-5-nitrophenyl sulfate
-
in presence of 400 mM acetate
0.0486
2-hydroxy-5-nitrophenyl sulfate
-
in presence of 25-400 mM acetate
0.085
2-hydroxy-5-nitrophenyl sulfate
-
in presence of 100 mM acetate and 100 mM sulfate
0.55
2-methyl-4-nitrophenyl sulfate
-
pH 8.9, 30C
0.123
4-hydroxy-2-nitrophenyl sulfate
-
in presence of 100 mM acetate
0.193
4-hydroxy-3-nitrophenyl sulfate
-
in presence of 100 mM acetate
2.5
4-methylumbelliferone sulfate
-
-
0.0066
4-Methylumbelliferyl sulfate
-
pH 8.9, 30C
0.105
4-nitrocatechol sulfate
-
-
0.16
4-nitrocatechol sulfate
-
-
0.166
4-nitrocatechol sulfate
-
beta enzyme
0.2
4-nitrocatechol sulfate
-
enzyme from fraction II and fraction III
0.204
4-nitrocatechol sulfate
-
alpha enzyme
0.21
4-nitrocatechol sulfate
-
pH 5.0, 37C, wild-type
0.23
4-nitrocatechol sulfate
-
enzyme from fraction I
0.25
4-nitrocatechol sulfate
-
0.25 M acetate buffer, pH 5.0
0.26
4-nitrocatechol sulfate
-
pH 5.0, 37C, patient with cerebral palsy
0.3
4-nitrocatechol sulfate
-
-
0.5
4-nitrocatechol sulfate
-
0.25 M acetate buffer, pH 5.6
0.68
4-nitrocatechol sulfate
-
arylsulfatase B
1.1
4-nitrocatechol sulfate
-
-
1.8
4-nitrocatechol sulfate
-
arylsulfatase A
2.5
4-nitrocatechol sulfate
-
-
2.9
4-nitrocatechol sulfate
-
arylsulfatase B
3.2
4-nitrocatechol sulfate
-
arylsulfatase A
6
4-nitrocatechol sulfate
-
pH 7.5, 45C
10.9
4-nitrocatechol sulfate
Q6UWY0
pH 4.6, 37C
20.6
4-nitrocatechol sulfate
Q6UWY0
pH 4.6, 37C
0.0291
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25C
0.0752
4-nitrophenyl phosphate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25C
0.00025
4-nitrophenyl sulfate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25C
0.00029
4-nitrophenyl sulfate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25C
0.0004
4-nitrophenyl sulfate
-
mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25C
0.0037
4-nitrophenyl sulfate
-
in presence of 1 mM CaCl2
0.017
4-nitrophenyl sulfate
-
in absence CaCl2
0.0294
4-nitrophenyl sulfate
-
alpha enzyme
0.042
4-nitrophenyl sulfate
-
pH 8.9, 30C
0.07
4-nitrophenyl sulfate
-
without imidazole
0.075
4-nitrophenyl sulfate
-
beta enzyme
0.08
4-nitrophenyl sulfate
-
-
0.2
4-nitrophenyl sulfate
-
with imidazole
0.27
4-nitrophenyl sulfate
-
-
0.3
4-nitrophenyl sulfate
-
-
0.53
4-nitrophenyl sulfate
-
-
0.59
4-nitrophenyl sulfate
-
-
0.82
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 160 MPa
1.12
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 120 MPa
1.2
4-nitrophenyl sulfate
-
pH 7.08, 30C
1.5 - 2
4-nitrophenyl sulfate
-
pH 7.4, 24.85C, pressure: 0.1 MPa
1.6
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 5 MPa
1.61
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 40 MPa
1.62
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 80 MPa
1.85
4-nitrophenyl sulfate
-
pH 7.43, 30C
2.01
4-nitrophenyl sulfate
-
pH 7.4, 19.85C, pressure: 0.1 MPa
2.12
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 0.1 MPa
2.31
4-nitrophenyl sulfate
-
pH 7.4, 22.35C, pressure: 0.1 MPa
2.47
4-nitrophenyl sulfate
-
pH 7.4, 14.85C, pressure: 0.1 MPa
2.49
4-nitrophenyl sulfate
-
pH 7.4, 17.35C, pressure: 0.1 MPa
2.5
4-nitrophenyl sulfate
-
pH 7.4, 34.85C, pressure: 0.1 MPa
4.36
4-nitrophenyl sulfate
-
pH 8.08, 30C
5.26
4-nitrophenyl sulfate
-
pH 8.68, 30C
26
4-nitrophenyl sulfate
-
-
0.5
Ascorbate 2-sulfate
-
-
2.5
Ascorbic acid 2-sulfate
-
-
0.13
cerebroside 3-sulfate
-
-
7.2
dopamine 3-sulfate
-
pH 6.9
9.8
dopamine 3-sulfate
-
pH 7.4
2.1
dopamine 4-sulfate
-
pH 6.9
2.8
dopamine 4-sulfate
-
pH 7.4
14.1
epinephrine 3-sulfate
-
pH 6.9
18
epinephrine 3-sulfate
-
pH 7.4
1.9
epinephrine 4-sulfate
-
pH 6.9
2.5
epinephrine 4-sulfate
-
pH 7.4
0.344
Estrone 3-sulfate
-
-
1.05
N-benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate
-
-
10.5
norepinephrine 3-sulfate
-
pH 6.9
12.8
norepinephrine 3-sulfate
-
pH 7.4
2.7
norepinephrine 4-sulfate
-
pH 6.9
3.3
norepinephrine 4-sulfate
-
pH 7.4
0.0549
p-Nitrophenyl sulfate
-
-
0.67
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase incubated at 45C and at pH 7.0 in the presence of 10 mM sulfate
1.15
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase incubated at 45C and at pH 7.0
8.7
p-Nitrophenyl sulfate
Littorina kurila
-
37C, pH 5.4
3.65
phloroglucinol monosulfate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000095
4-nitrophenyl phosphate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25C
0.023
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25C
0.000061
4-nitrophenyl sulfate
-
mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25C
0.0054
4-nitrophenyl sulfate
-
mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25C
14.2
4-nitrophenyl sulfate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25C
40.5
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 120 MPa
41.83
4-nitrophenyl sulfate
-
pH 7.4, 17.35C, pressure: 0.1 MPa
42.5
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 160 MPa
42.83
4-nitrophenyl sulfate
-
pH 7.4, 14.85C, pressure: 0.1 MPa
46.16
4-nitrophenyl sulfate
-
pH 7.4, 19.85C, pressure: 0.1 MPa
46.5
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 40 MPa
48.33
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 5 MPa
51.33
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 80 MPa
56.33
4-nitrophenyl sulfate
-
pH 7.4, 24.85C, pressure: 0.1 MPa
58
4-nitrophenyl sulfate
-
pH 7.4, 22.35C, pressure: 0.1 MPa
74.5
4-nitrophenyl sulfate
-
pH 7.4, 29.85C, pressure: 0.1 MPa
90.83
4-nitrophenyl sulfate
-
pH 7.4, 34.85C, pressure: 0.1 MPa
1000
p-Nitrophenyl sulfate
-
6.5 nM purified arylsulfatase, at 45C and pH 7.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.302
2-(difluoromethyl)phenyl hydrogen sulfate
-
pH 8.9, 30C
0.975
3,4-dihydro-1,2,3-benzoxathiazine 2,2-dioxide
-
pH 8.9, 30C
0.401
3H-1,2,3-benzoxathiazole 2,2-dioxide
-
pH 8.9, 30C
0.029
4-(difluoromethyl)phenyl hydrogen sulfate
-
pH 8.9, 30C
0.0292
4-nitrophenyl phosphate
-
wild type enzyme, in 100 mM Tris, pH 8.0, 25C
0.0045
phenyl sulfamate
-
pH 8.9, 30C
0.00055
praziquantel
-
pH 6.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
phosphate
-
at 10 mM 4-nitrocatechol sulfate
2.4
phosphate
Q6UWY0
pH 4.6, 37C
0.001
sulfate
-
at 10 mM 4-nitrocatechol sulfate
2.9
sulfate
Q6UWY0
pH 4.6, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.93
-
substrate agar
4.07
-
arylsulfatase B
4.82
-
arylsulfatase A
97.2
-
substrate p-nitrophenyl sulfate
113
-
maximal specific activity using p-nitrophenyl sulfate
468
-
7.1 mM p-nitrophenyl sulfate at 45C and at pH 8.5, after Heparin-Sepharose column chromatography
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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
-
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
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 50C results in a decrease of activity by about 50%
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
-
0.00003 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 mol/min/mL was measured at 50 mM p-nitrophenyl sulfate, pH 8.5 and 40C, with 10 M IPTG
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2 - 4.7
-
hydrolysis of ascorbic acid 2-sulfate
4.3
-
hydrolysis of 4-nitrocatechol sulfate
4.6
Q6UWY0
-
4.8
-
hydrolysis of cerebroside 3-sulfate
4.8
-
20 mM p-nitrocatechol sulfate as substrate
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
5.2
-
arylsulfatase A
5.4
-
120 min incubation in presence of NaCl
5.4
-
for the reaction with 4-nitrocatechol sulfate
5.5 - 6
-
4-nitrophenyl sulfate
5.5
-
hydrolysis of 2-hydroxy-5-nitrophenyl sulfate in acetic acid/sodium acetate buffer
5.5
-
hydrolysis of 4-nitrocatechol sulfate
5.6
-
arylsulfatase B
5.6
-
hydrolysis of 3-nitrocatechol sulfate
5.6
-
for the reaction with 4-methylumbelliferyl sulfate
5.8
-
10 min incubation in presence of NaCl
6 - 6.2
-
hydrolysis of 4-methylumbelliferone sulfate
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
-
120 min incubation in presence of K2SO4
6.1
-
hydrolysis of 4-nitrocatechol sulfate
6.2
-
10 min incubation in presence of K2SO4
6.2
-
4 mM p-nitrocatechol sulfate as substrate
6.5
-
hydrolysis of 4-nitrophenyl sulfate in acetate buffer
6.5
-
hydrolysis of 4-nitrophenyl sulfate
6.8 - 8.2
-
-
7
-
activity of purified arylsulfatase analysed at 40C and at pH 4.5 to 10, p-nitrophenyl sulfate as substrate
7.4
-
assay at
8.4
-
hydrolysis of 4-nitrophenyl sulfate, beta enzyme; hydrolysis of nitrocatechol sulfate, beta enzyme
8.8
-
hydrolysis of 4-nitrocatechol sulfate, alpha enzyme
9
-
hydrolysis of 4-nitrophenyl sulfate, alpha enzyme
9
-
with imidazole
9
-
enzyme ES-2
9.8
-
without imidazole
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
4 - 7
-
pH 4: about 15% of maximal activity, pH 7.0: about 55% 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; pH 5.0: about 75% of maximal activity, pH 7.0: about 45% of maximal activity, hydrolysis of 4-nitrocatechol sulfate
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
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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
enzyme Es-2
30
-
assay at
37
-
enzyme Es-1
45 - 50
-
ASG cleaves 4-nitrocatechol sulfate most efficiently at 45-50C
45
-
purified arylsulfatase analysed at pH 7.0 and temperature between 10 to 80C, p-nitrophenyl sulfate as substrate
additional information
Littorina kurila
-
50% loss in activity at 60C compared to control condition of 37C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
14% residual activity
4 - 50
-
4C: about 40% of maximal activity, 50C: about 45% of maximal activity
4 - 50
-
4C: about 40% of maximal activity, 50C: about 25% of maximal activity, enzyme ES-2
10 - 60
-
10C: about 35% of maximal activity, 60C: about 30% of maximal activity
40 - 65
-
40C: about 40% of maximal activity, 65C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme expression is unaltered in cancer tissue compared to nonmalignant tissue
Manually annotated by BRENDA team
-
activity increases gradually during development
Manually annotated by BRENDA team
-
no significant changes in enzyme level upon feeding ethanol-containing Lieber-DeCarli liquid diet
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
primary epithelial cell, highest activity of galacose 6-sulfatase and aryl sulfatase B of all the cell lines tested
Manually annotated by BRENDA team
Q3TYD4
poor expression
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
no significant changes in enzyme level upon feeding ethanol-containing Lieber-DeCarli liquid diet
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
enzyme activity is elevated in mouse schistosomiasis
Manually annotated by BRENDA team
-
enzyme level decreases in animals receiving ethanol-containing Lieber-DeCarli liquid diet compared with control diet
Manually annotated by BRENDA team
-
In the sinusoidal endothelial cells, both surfaces of the luminal side and outside of sinusoid are positively stained
Manually annotated by BRENDA team
Q3TYD4
poor expression
Manually annotated by BRENDA team
-
enzyme expression is unaltered in breast cancer tissue compared to nonmalignant tissue
Manually annotated by BRENDA team
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
Manually annotated by BRENDA team
-
raw milk or pasteurized milk incubated at 60C for 30 min
Manually annotated by BRENDA team
-
primary myoepithelial cell, highest activity of steryl sulfatase and aryl sulfatase B of all the cell lines tested
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
Q6UWY0
high level of expression
Manually annotated by BRENDA team
Q6UWY0
high level of expression
Manually annotated by BRENDA team
-
placental membrane, far from and close to internal uterine os
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
P70 is present on capacitated cauda sperm surface
Manually annotated by BRENDA team
-
activity increases gradually during development
Manually annotated by BRENDA team
-
remarkably low activity of arylsulfatase A, arylsulfatase B, galacose 6-sulfatase and steryl sulfatase, but not iduronate 2-sulfatase
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
raw milk or pasteurized milk which was incubated at 60C for 30 min
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
sulfatase mRNA expression levels in 13 malignant and nonmalignant tissue samples, overview
Manually annotated by BRENDA team
additional information
Q6UWY0
mRNA expression is found in all tissues tested
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
J9QRU6
32% of arylsulfatase acivity is intracellular
Manually annotated by BRENDA team
-
32% of arylsulfatase acivity is intracellular
-
Manually annotated by BRENDA team
-
inside membrane-bound cytoplasmic vesicles
Manually annotated by BRENDA team
-
inside membrane-bound cytoplasmic vesicles distributed throughout the cell body
Manually annotated by BRENDA team
Q3TYD4
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
Manually annotated by BRENDA team
Q6UWY0
protein carries mannose 6-phosphate, indicating lysosomal sorting
Manually annotated by BRENDA team
Q3TYD4
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
Manually annotated by BRENDA team
J9QRU6
68% of arylsulfatase acivity is membrane-associated
Manually annotated by BRENDA team
J9QXV9
99% of arylsulfatase activity is membrane-associated
Manually annotated by BRENDA team
J9QWA6
99% of arylsulfatase activity is membrane-associated
Manually annotated by BRENDA team
-
99% of arylsulfatase activity is membrane-associated
-
Manually annotated by BRENDA team
-
68% of arylsulfatase acivity is membrane-associated
-
Manually annotated by BRENDA team
-
P70 is present mainly in the acrosomal soluble fraction
-
Manually annotated by BRENDA team
-
99% of arylsulfatase activity is membrane-associated
-
Manually annotated by BRENDA team
additional information
-
enzyme is not secreted by epimastigote or trypomastigote form and not detected in epimastigote reservosome
-
Manually annotated by BRENDA team
additional information
-
immunohistochemic localization analysis, overview. ARSA and ARSB are also colocalized with heparan sulfate proteoglycan
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
-
SDS-PAGE
669821
33000
-
SDS-PAGE
670770
39000
-
gel filtration
135531
40000
-
the enzyme has the ability to complex to molecular masses of more than 300000, gel filtration
135534
41000
-
gel permeation chromatography
667275
45000
-
gel filtration
135516
45000
Littorina kurila
-
SDS-PAGE
667914
49000
-
gel filtration
135519
49000
-
gel filtration
135522
51000
-
arylsulfatase B, gel filtration
135529
59000
-
enzyme from fraction II, gel filtration
135528
60000
-
SDS-PAGE
692779
62000
-
SDS-PAGE
667275
63000
-
SDS-PAGE
693036
68000
-
immunoblot
668717
70000
-
SDS-PAGE
694140
94000
-
enzyme from fraction I, gel filtration
135528
94900
-
sedimentation equilibrium
135512
97000
-
gel filtration
135522
100000
-
gel filtration
135513
100000
-
gel filtration
135527
105000
-
enzyme from fraction III, gel filtration
135528
107000
-
arylsulfatase A, gel filtration
135529
150000
-
gel filtration, ultracentrifugation
135515
166000
-
gel filtration
135530
349000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
675156
460000
-
one of two molecular forms consisting of identical subunits with molecular mass of 53000 Da
675156
670000
-
gel filtration
135526
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 53000
?
-
x * 56000, ARSA, SDS-PAGE
?
-
x * 64000, ARSB, SDS-PAGE
?
Q6UWY0
x * 68000, SDS-PAGE of recombinant glycoprotein, cellular form, x * 70000, SDS-PAGE of recombinant glycoprotein, secreted form
decamer
-
10 * 63000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 46000, SDS-PAGE
monomer
-
1 * 46500, SDS-PAGE
monomer
-
1 * 57000, SDS-PAGE
monomer
-
1 * 63000, active enzyme, SDS-PAGE
monomer
Streptomyces sp. T109-3
-
1 * 46500, SDS-PAGE
-
additional information
-
enzyme has a specific affinity for chondroitin sulfate B, a component of the cumulus matrix proteoglycan network
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
contains complex N-linked oligosaccharides
proteolytic modification
-
the enzyme is synthesized as a higher molecular mass precursor
no modification
-
not a glycoprotein
glycoprotein
-
-
glycoprotein
-
-
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
-
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
Q3TYD4
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
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
glycoprotein
Q6UWY0
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
additional information
Q3TYD4
presence of a disulfide bridge between the processed 18-kDa fragment and another smaller polypeptide, probably involving residue Cys195 of the 10-kDa chain
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
below pH 4 in presence of 1% SDS arylsulfatase A is irreversibly converted into inactive subunits
135529
5.5
-
rapid loss of activity below
135535
6
-
rapid inactivation below
135520
6.5 - 10
-
stable
135514
8 - 10
-
stable
135520
8 - 9.5
-
37C, 30 min, most stable
135518
8 - 9.5
-
enzyme ES-2, stable
135535
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
stable for 2 h
675156
20
-
arylsulfatase III, stable for 1 h, unstable above
135520
22
-
stable at room temperature
135530
30 - 40
-
5 min, in presence of substrate, stable
135514
30
-
enzyme Es-2, stable below
135535
30
-
3 h, stable up to
678774
37
-
5 h, 30% loss of activity
135534
40
-
30 min, stable below
135518
50
-
30 min, about 50% loss of activity
135518
55
-
ASG activity is retained even at relatively high temperatures above 55C
693036
56
-
5 h, 51% loss of activity
135534
60
-
rapidly inactivated at alkaline and acid pH, more thermostable at pH 6.5-7.0
135515
60
-
5 min, about 50% loss of activity
135516
60
-
40 min, 70% loss of activity
135524
70
-
30 min, complete loss of activity
135518
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
several cycles of freezing and thawing cause a marked reduction of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 8 weeks, about 80% loss of activity
-
3C, 0.1 M sodium phosphate buffer, 14 days, 25% loss of activity
-
-20C, 2 days, 60% loss of activity
-
-20C, stable for 2 months
-
4C, pH 6.0, half-life of more than 100 days
-
4C, stable for 24 h
-
-20C, stable for several months
-
-20C, stable for more than 6 months
-
0C, without freezing, 72 h, inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
strain R-0827, partial, arylsulfatase III
-
strain SH 10-6, partial, arylsulfatase III
-
partial
-
use of solid phase extraction on a polymeric resin for purification without affecting the enzyme activity
-
type II arylsulfatase
-
arylsulfatase A and B
-
Ni-NTA column chromatography and HisTrap column chromatography
-
retroviral expressed enzyme purified with ion-exchange DEAE-cellulose chromatography followed by immuno-affinity purification using a polyclonal antibody against arylsulfatase A sequence
-
gel filtration on a Sepharose CL 6B column under elution with 0.025 M acetate buffer, pH 5.4
Littorina kurila
-
from liver of Schistosoma-infected animal
-
DEAE-cellulose anion-exchange and Heparin-Sepharose CL 6B affinity chromatography, all steps at 4C
-
arylsulfatase Es-1
-
arylsulfatase Es-2
-
partial, arylsulfatase A and B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
-
ARS-A and ARS-B, quantitative real-time RT-PCR expression analysis
-
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
-
expressed in COS-7 cells
-
expressed in HT-1080 cells
-
expression in HEK-293 cells
Q6UWY0
retroviral expression system
-
expression in HT-1080 cells
Q3TYD4
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
-
overexpression in E.coli BL21
-
overexpression in Escherichia coli BL21
-
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
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
J9QXV9
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
J9QXV9
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
-
-
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
J9QWA6
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
J9QWA6
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
-
-
no enzymic activity is measured when microorganisms are present in a medium supplemented with inorganic sulfate as sole sulfur source
J9QRU6
enzymic activity is detected when microorganisms are grown in sulfate-limiting conditions
J9QRU6
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
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C80A
Q6UWY0
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
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
N215Q
Q3TYD4
residue Asn215 functions as glycosylation site
N356Q
Q3TYD4
residue Asn356 functions as glycosylation site
N497Q
Q3TYD4
mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification
C51A
-
mutant with strongly reduced activity
C51S
-
mutant with strongly reduced activity
I40S
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
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 5065% of injected hemisphere
W124G
-
naturally occurring missense mutation causing ARSA deficiency, isolated from two Tunisian patients with late infantile metachromatic leukodystrophy, MLD
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%
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
cytochemical localization of enzyme in cytoplasmic vesicles as a specific detection method for lysosomes
medicine
-
use of immobilized and column-packed enzyme is an efficient alternative for the cleavage of urinary conjugates in clinical toxicology
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
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
P15848
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
-
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
-
the enzyme can be accepted as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy
medicine
Streptomyces sp. T109-3
-
the enzyme can be accepted as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy
-
analysis
-
distinction of lysosomes and reservosomes by cytochemical localization of enzyme in epimastigote and trypomastigote