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Information on EC 3.1.6.1 - arylsulfatase (type I)
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3.1.6.1 arylsulfatase (type I)IUBMB Comments
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, formylglycine-generating enzyme, EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
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Word Map
- 3.1.6.1
- lysosomal
-
metachromatic
- leukodystrophy
- beta-glucuronidase
- steroid
- urine
- mucopolysaccharidosis
- sulfatide
- leukocyte
- urinary
- asa
- estrone
- glycosaminoglycans
-
glucuronide
- demyelination
- cerebroside
- urease
-
sulfotransferase
- aromatase
- heparan
- beta-glucosidase
-
desulfation
- dehydroepiandrosterone
- dermatan
-
infantile
-
17beta-hydroxysteroid
-
mucopolysaccharide
- pomatia
- ichthyosis
- hexosaminidase
- morquio
-
saposins
-
iduronate
- 17beta-hsds
- galactosylceramide
- alpha-fucosidase
-
chondrodysplasia
-
hspgs
- synthesis
- medicine
-
deconjugation
- analysis
-
6-o-sulfate
- tibolone
- alpha-l-iduronidase
-
loam
-
sanfilippo
- galns
- punctata
- mucolipidosis
- sulfamate
- 4-sulfate
- dysostosis
The enzyme appears in viruses and cellular organisms
Synonyms
sulfatase, arylsulfatase a, arylsulfatase, arylsulphatase, arylsulfatase b, arylsulphatase a, estrogen sulfatase, ars-a, arylsulfatase e, arylsulfatase g, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methylumbelliferyl sulfatase
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ARS
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ARSA
ARSB
Aryl-sulfate sulphohydrolase
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-
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arylsulfatase
arylsulfatase A
arylsulfatase B
arylsulfatase Es-2
arylsulfatase G
arylsulfohydrolase
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-
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-
arylsulphatase
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-
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-
arylsulphatase A
AtsA
estrogen sulfatase
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-
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nitrocatechol sulfatase
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-
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p-nitrophenyl sulfatase
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P70
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the protein inhibits Na+,K+-ATPase activity and shows strong arylsulphatase A like activity
phenolsulfatase
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phenylsulfatase
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-
-
sulfatase
sulfatase, aryl-
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arylsulfatase
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-
-
sulfatase
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-
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aryl sulfate + H2O = a phenol + sulfate
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-
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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
Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, formylglycine-generating enzyme, EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
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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
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-
-
-
?
2-fluoro-4-nitrophenyl sulfate + H2O
2-fluoro-4-nitrophenol + sulfate
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-
-
?
2-hydroxy-4-nitrophenyl sulfate + H2O
2-hydroxy-4-nitrophenol + sulfate
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-
-
-
?
2-methyl-4-nitrophenyl sulfate + H2O
2-methyl-4-nitrophenol + sulfate
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-
-
-
?
3,4-dimethylphenyl sulfate + H2O
3,4-dimethylphenol + sulfate
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-
-
?
3,4-dinitrophenyl sulfate + H2O
3,4-dinitrophenol + sulfate
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-
-
?
3-fluoro-4-nitrophenyl sulfate + H2O
3-fluoro-4-nitrophenol + sulfate
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-
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?
3-indoxyl sulfate + H2O
1H-indol-3-ol + sulfate
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6.4% of the activity with 4-nitrophenyl sulfate
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?
4-hydroxy-2-nitrophenyl sulfate + H2O
4-hydroxy-2-nitrophenol + sulfate
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-
-
-
?
4-hydroxy-3-nitrophenyl sulfate + H2O
4-hydroxy-3-nitrophenol + sulfate
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-
-
-
?
6-benzoyl-2-naphthyl sulfate + H2O
6-benzoyl-2-naphthol + sulfate
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-
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?
benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate methyl ester + H2O
benzyloxycarbonyl-L-Phe-L-Tyr + methylsulfate
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-
-
-
?
epitestosterone 17-sulfate + H2O
epitestosterone + sulfate
reaction of EC 3.1.6.2
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-
?
etiocholanolone 3-sulfate + H2O
etiocholanolone + sulfate
reaction of EC 3.1.6.2
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-
?
methylumbelliferyl sulfate + H2O
methylumbelliferone + sulfate
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?
N-benzyloxycarbonyl-L-Phe-L-Tyr-O-sulfate + H2O
N-benzyloxycarbonyl-L-Phe-L-Tyr + -sulfate
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-
-
-
?
phloroglucinol monosulfate + H2O
phloroglucinol + sulfate
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-
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?
sulfated polysaccharide + H2O
polysaccharide + sulfate
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-
?
testosterone 17-sulfate + H2O
testosterone + sulfate
reaction of EC 3.1.6.2
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?
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
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?
2'',3''-di-O-acetyletoposide 4'-sulfate + H2O
2'',3''-di-O-acetyletoposide + sulfate
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?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
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?
2-hydroxy-5-nitrophenyl sulfate + H2O
2-hydroxy-5-nitrophenol + sulfate
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?
3-carboxyphenyl sulfate + H2O
3-carboxyphenol + sulfate
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weak activity
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?
3-carboxyphenyl sulfate + H2O
3-carboxyphenol + sulfate
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weak activity
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?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
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?
4-acetylphenyl sulfate + H2O
4-acetylphenol + sulfate
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
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rather poor substrate
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferol + sulfate
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
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-
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
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-
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
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-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
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?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
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-
-
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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77% of the activity with 4-nitrophenyl sulfate
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-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
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?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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-
?
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
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-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
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-
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?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
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-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
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-
-
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?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
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-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
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-
-
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?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
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-
-
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?
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
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-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
the 4-nitrocatechol sulfate substrate is hydrolyzed to a greater extent than the 4-nitrophenyl sulfate substrate
-
-
?