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EC Tree
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. This enzyme belongs to the type III sulfatase family. It is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 3.1.6.22, branched primary-alkylsulfatase, and EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a primary alkyl sulfate ester
+
=
+
Synonyms
sdsa1, sdsap, primary alkylsulfatase, type iii alkylsulfatase,
more
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type III linear primary-alkylsulfatase
-
-
-
-
RS2
-
-
sdsA1
-
-
-
-
sec-alkylsulfatase
-
-
type III alkylsulfatase
-
type III alkylsulfatase
-
-
yjcS
-
-
-
-
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a primary alkyl sulfate ester + H2O = an alcohol + sulfate
-
-
-
-
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primary alkyl sulfate ester 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. This enzyme belongs to the type III sulfatase family. It is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 3.1.6.22, branched primary-alkylsulfatase, and EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III).
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(+/-)-4-octyl sulfate + H2O
4-octanol + sulfate + H+
(R)-2-octyl sulfate + H2O
(S)-2-octanol + sulfate + H+
(R)-3-octyl sulfate + H2O
3-octanol + sulfate + H+
1-decane sulfonic acid + H2O
?
-
-
-
?
2-butyloctyl sulfate + H2O
2-butyloctanol + sulfate
-
-
-
-
?
decyl sulfate + H2O
decanol + sulfate
-
-
-
?
hexyl sulfate + H2O
hexanol + sulfate
-
-
-
?
mucin + H2O
? + sulfate
-
-
-
?
octyl sulfate + H2O
octanol + sulfate
-
-
-
?
SDS + H2O
1-dodecanol + sulfate + Na+
sodium octyl sulfate + H2O
1-octanol + sulfate + Na+
-
-
-
?
additional information
?
-
(+/-)-4-octyl sulfate + H2O
4-octanol + sulfate + H+
-
-
-
-
?
(+/-)-4-octyl sulfate + H2O
4-octanol + sulfate + H+
-
-
-
-
?
(R)-2-octyl sulfate + H2O
(S)-2-octanol + sulfate + H+
-
when (+/-)-2-octyl sulfate is used as a substrate, the enzyme shows a clear preference for (R)-2-octyl sulfate
-
-
?
(R)-2-octyl sulfate + H2O
(S)-2-octanol + sulfate + H+
-
when (+/-)-2-octyl sulfate is used as a substrate, the enzyme shows a clear preference for (R)-2-octyl sulfate
-
-
?
(R)-3-octyl sulfate + H2O
3-octanol + sulfate + H+
-
when (+/-)-3-octyl sulfate is used as a substrate, the enzyme shows a clear preference for (R)-3-octyl sulfate
-
-
?
(R)-3-octyl sulfate + H2O
3-octanol + sulfate + H+
-
when (+/-)-3-octyl sulfate is used as a substrate, the enzyme shows a clear preference for (R)-3-octyl sulfate
-
-
?
SDS + H2O
1-dodecanol + sulfate + Na+
-
-
-
?
SDS + H2O
1-dodecanol + sulfate + Na+
-
-
-
?
SDS + H2O
1-dodecanol + sulfate + Na+
-
-
-
?
SDS + H2O
1-dodecanol + sulfate + Na+
-
-
-
?
additional information
?
-
D-glucosamine 2-sulfate, D-glucose 3-sulfate, 4-nitrocatecholsulfate and 4-nitrophenylsulfate are not cleaved by the enzyme
-
-
-
additional information
?
-
-
D-glucosamine 2-sulfate, D-glucose 3-sulfate, 4-nitrocatecholsulfate and 4-nitrophenylsulfate are not cleaved by the enzyme
-
-
-
additional information
?
-
-
no activity with SDS
-
-
-
additional information
?
-
-
the enzyme shows no activity with branched and mixed aryl-alkyl sec-sulfates
-
-
-
additional information
?
-
-
the enzyme shows no activity with branched and mixed aryl-alkyl sec-sulfates
-
-
-
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mucin + H2O
? + sulfate
-
-
-
?
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additional information
not activated by Na+, K+, and Mg2+
Ca2+
activates
Ca2+
100.3% activity at 100 mM
Zn2+
contains zinc
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Cu2+
82.9% residual activity at 10 mM
EDTA
25.8% residual activity at 10 mM
Fe2+
55.4% residual activity at 10 mM
Co2+
-
Co2+
68.7% residual activity at 10 mM
Mn2+
-
Mn2+
66.1% residual activity at 10 mM
Zn2+
-
Zn2+
77.8% residual activity at 10 mM
additional information
not inhibited by dithiothreitol and 2-mercaptoethanol
-
additional information
-
addition of EDTA does not eliminate enzyme activity
-
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Urea
100.2% activity at 10 mM
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0.009
SDS
at pH 7.5 and 25°C
0.0742
SDS
at pH 7.1 and 25°C
0.2643
SDS
at pH 9.0 and 70°C
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4.88
SDS
at pH 7.1 and 25°C
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0.058
-
cell extract, at pH 7.5 and 30°C
23.25
purified recombinant enzyme, at pH 9.0 and 70°C
6.88
-
after 119fold purification, at pH 7.5 and 30°C
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6.5 - 9
-
more than 50% activity between pH 6.5 and 9.0
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20 - 35
-
about 50% activity at 20°C, about 60% activity at 25°C, 100% activity at 30°C, about 20% activity at 35°C, no activity at 40°C
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5.1
-
isoelectric focusing
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UniProt
brenda
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UniProt
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no activity in Pseudomonas sp. C12B
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-
brenda
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UniProt
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-
-
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UniProt
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brenda
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-
-
brenda
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brenda
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brenda
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malfunction
the sdsA1 mutant shows a reduction in the ability of mucin gel penetration and an attenuation of virulence in leukopenic mice compared with the wild type strain
physiological function
the enzyme plays an important role as a virulence factor of Pseudomonas aeruginosa
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LPAKS_ECOLI
Escherichia coli (strain K12)
661
0
73151
Swiss-Prot
-
LPAKS_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
658
0
72592
Swiss-Prot
-
LPAKS_PSES9
528
0
58950
Swiss-Prot
-
LPAKS_PSESP
674
0
75040
Swiss-Prot
-
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homodimer
2 * 70000, SDS-PAGE
homodimer
2 * 73000, calculated from amino acid sequence
homodimer
-
2 * 70000, SDS-PAGE
-
homodimer
-
2 * 73000, calculated from amino acid sequence
-
homodimer
2 * 70000, SDS-PAGE
homodimer
2 * 74900, calculated from amino acid sequence
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
-
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hanging drop vapor diffusion method, using 1.8M (NH4)2SO4, 2% (w/v) PEG400, and 0.1M HEPES (pH 7.4)
apoenzyme and complexes with substrate analog and products, hanging drop vapor diffusion method, using 12% (w/v) PEG 4000, 10% isopropanol, 200 mM LiCl, 100 mM sodium citrate, pH 6.0
sitting drop vapor diffusion method, using 0.1 M sodium acetate (pH4.5), 0.05 M magnesiumacetate, 20% (w/v) polyethylene glycol 4000
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G263A
the mutation reduces the enzyme activity for SDS degradation to less than 20% of wild type activity
G263F
the mutation reduces the enzyme activity for SDS degradation to less than 20% of wild type activity
Y246A
the mutation reduces the enzyme activity for SDS degradation to less than 20% of wild type activity
Y246A/G263A
the mutation reduces the enzyme activity for SDS degradation to less than 20% of wild type activity
Y246S
the mutation reduces the enzyme activity for SDS degradation to less than 20% of wild type activity
Y246S/G263F
completely inactive
D184N/H185A
inactive
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6 - 11
the enzyme retains more than 90% activity after incubation at a wide pH range of 6.0-11.0 for 1 h
761050
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65
the enzyme keeps more than 90% activity after treatment at 65°C for 1 h
65
the enzyme retains more than 90% activity after incubation at 60 and 65°C for 1 h
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DEAE-cellulose column chromatography, phenyl Sepharose column chromatography, Q6 column chromatography, Blue Sepharose column chromatography, and Superdex 200 gel filtration
-
IMAC column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography, Mono Q column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Tuner cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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Ellis, A.J.; Hales, S.G.; Ur-Rehman, N.G.; White, G.F.
Novel alkylsulfatases required for biodegradation of the branched primary alkyl sulfate surfactant 2-butyloctyl sulfate
Appl. Environ. Microbiol.
68
31-36
2002
no activity in Pseudomonas sp. C12B, Pseudomonas sp. AE-A
brenda
Pogorevc, M.; Faber, K.
Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541
Appl. Environ. Microbiol.
69
2810-2815
2003
Rhodococcus ruber, Rhodococcus ruber DSM 44541
brenda
Sun, L.; Chen, P.; Su, Y.; Cai, Z.; Ruan, L.; Xu, X.; Wu, Y.
Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9
Biosci. Rep.
37
BSR20170001
2017
Pseudomonas sp. S9 (F2WP51)
brenda
Long, M.; Ruan, L.; Li, F.; Yu, Z.; Xu, X.
Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP)
Extremophiles
15
293-301
2011
Pseudomonas sp. S9 (F2WP51)
brenda
Kida, Y.; Yamamoto, T.; Kuwano, K.
SdsA1, a secreted sulfatase, contributes to the in vivo virulence of Pseudomonas aeruginosa in mice
Microbiol. Immunol.
64
280-295
2020
Pseudomonas aeruginosa (Q9I5I9), Pseudomonas aeruginosa
brenda
Hagelueken, G.; Adams, T.M.; Wiehlmann, L.; Widow, U.; Kolmar, H.; Tuemmler, B.; Heinz, D.W.; Schubert, W.D.
The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases
Proc. Natl. Acad. Sci. USA
103
7631-7636
2006
Pseudomonas aeruginosa (Q9I5I9), Pseudomonas aeruginosa
brenda
Liang, Y.; Gao, Z.; Dong, Y.; Liu, Q.
Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase
Protein Sci.
23
1442-1450
2014
Escherichia coli (P32717), Escherichia coli, Escherichia coli DH5alpha (P32717)
brenda
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