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Information on EC 3.1.6.1 - arylsulfatase (type I) and Organism(s) Pseudomonas aeruginosa and UniProt Accession P51691
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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 taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
sulfatase, arylsulfatase a, arylsulfatase, arylsulphatase, arylsulfatase b, arylsulphatase a, estrogen sulfatase, ars-a, arylsulfatase e, arylsulfatase g, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methylumbelliferyl sulfatase
-
-
-
-
ARS
-
-
-
-
Aryl-sulfate sulphohydrolase
-
-
-
-
arylsulfatase
-
-
-
-
arylsulfohydrolase
-
-
-
-
arylsulphatase
-
-
-
-
estrogen sulfatase
-
-
-
-
nitrocatechol sulfatase
-
-
-
-
p-nitrophenyl sulfatase
-
-
-
-
phenolsulfatase
-
-
-
-
phenylsulfatase
-
-
-
-
sulfatase
-
-
-
-
sulfatase, aryl-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY
9016-17-5
-
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
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
-
-
?
androsterone 3-sulfate + H2O
androsterone + 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
-
-
?
epitestosterone 17-sulfate + H2O
epitestosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
estrone 3-sulfate + H2O
estrone + sulfate
reaction of EC 3.1.6.2
-
-
?
etiocholanolone 3-sulfate + H2O
etiocholanolone + sulfate
reaction of EC 3.1.6.2
-
-
?
testosterone 17-sulfate + H2O
testosterone + sulfate
reaction of EC 3.1.6.2
-
-
?
2-methyl-4-nitrophenyl sulfate + H2O
2-methyl-4-nitrophenol + sulfate
-
-
-
-
?
4-methylumbelliferyl sulfate + H2O
4-methylumbelliferone + sulfate
-
-
-
-
?
4-nitrocatechol sulfate + H2O
4-nitrocatechol + sulfate
-
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
-
-
-
-
?
additional information
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
?
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
-
-
?
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
?
-
-
AtsBCA is controlled by CysB protein (a LysR-type transcriptional activator) in Pseudomonas aeruginosa
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
sulfate
-
activates hydrolysis of 4-nitrophenyl sulfate with the beta enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25°C
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, 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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 65
-
40°C: about 40% of maximal activity, 65°C: about 60% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
enzyme hydrolyzes dehydroepiandrosterone 3-sulfate and epiandrosterone 3-sulfate in a urine matrix. Purified arylsulfatase contains only sulfatase activity allowing for the selective hydrolysis of sulfate esters in the presence of glucuronide conjugates. The enzyme can be employed for short three-step chemoenzymatic synthesis of 5alpha-androstane-3beta,17beta-diol 17-glucuronide from epiandrosterone 3-sulfate
analysis
-
high-throughput screen for mutants expressed in Escherichia coli. The alkaline lysis buffer is 1.0 M Tris-HCl at pH 9.0 plus 0.1 % Tween-20 and 2.0 mM 4-aminobenzamidine, mixed with cell suspension at 8:1 to 12:1 ratio for continuous agitation of mixtures in 96-well plates under room temperature. The enzmye tolerates final 0.1 % Tween-20, and activities in lysates are steady from 3 to 9 h and comparable to sonication treatment but better than freezing-thawing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Delisle, G.J.; Milazzo, F.H.
Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa
Can. J. Microbiol.
18
561-568
1972
Pseudomonas aeruginosa
Beil, S.; Kehrli, H.; James, P.; Staudenmann, W.; Cook, A.M.; Leisinger, T.; Kertesz, M.A.
Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA)
Eur. J. Biochem.
229
385-294
1995
Pseudomonas aeruginosa
Hummerjohann, J.; Laudenbach, S.; Retey, J.; Leisinger, T.; kertesz, M.A.
The sulfur-regulated arylsulfatase gene cluster of Pseudomonas aeruginosa, a new member of the cys regulon
J. Bacteriol.
182
2055-2058
2000
Pseudomonas aeruginosa
Dierks, T.; Miech, C.; Hummerjohann, J.; Schmidt, B.; Kertesz, M.A.; von Figura, K.
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine
J. Biol. Chem.
273
25560-25564
1998
Pseudomonas aeruginosa
Boltes, I.; Czapinska, H.; Kahnert, A.; von Bulow, R.; Dierks, T.; Schmidt, B.; von Figura, K.; Kertesz, M.A.; Uson, I.
1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
Structure
9
483-491
2001
Pseudomonas aeruginosa (P51691), Pseudomonas aeruginosa
Hanson, S.R.; Whalen, L.J.; Wong, C.H.
Synthesis and evaluation of general mechanism-based inhibitors of sulfatases based on (difluoro)methyl phenyl sulfate and cyclic phenyl sulfamate motifs
Bioorg. Med. Chem.
14
8386-8395
2006
Pseudomonas aeruginosa
Olguin, L.F.; Askew, S.E.; ODonoghue, A.C.; Hollfelder, F.
Efficient catalytic promiscuity in an enzyme superfamily: An arylsulfatase shows a rate acceleration of 10(13) for phosphate monoester hydrolysis
J. Am. Chem. Soc.
130
16547-16555
2008
Pseudomonas aeruginosa
Marino, T.; Russo, N.; Toscano, M.
Catalytic mechanism of the arylsulfatase promiscuous enzyme from Pseudomonas aeruginosa
Chemistry
19
2185-2192
2013
Pseudomonas aeruginosa (P51691), Pseudomonas aeruginosa
Yuan, M.; Yang, X.; Li, Y.; Liu, H.; Pu, J.; Zhan, C.G.; Liao, F.
Facile alkaline lysis of Escherichia coli cells in high-throughput mode for screening enzyme mutants arylsulfatase as an example
Appl. Biochem. Biotechnol.
179
545-557
2016
Pseudomonas aeruginosa
Stevenson, B.J.; Waller, C.C.; Ma, P.; Li, K.; Cawley, A.T.; Ollis, D.L.; McLeod, M.D.
Pseudomonas aeruginosa arylsulfatase a purified enzyme for the mild hydrolysis of steroid sulfates
Drug Test. Anal.
7
903-911
2015
Pseudomonas aeruginosa (P51691), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (P51691)
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