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Information on EC 3.1.6.21 - linear primary-alkylsulfatase
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3.1.6.21 linear primary-alkylsulfataseIUBMB 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).
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a primary alkyl sulfate ester
+
=
+
Synonyms
sdsa1, sdsap, primary alkylsulfatase, type iii alkylsulfatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RS2
sdsA1
sec-alkylsulfatase
type III alkylsulfatase
type III linear primary-alkylsulfatase
-
-
-
-
yjcS
sdsA1
-
-
-
-
yjcS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alkyl sulfate ester + H2O = an alcohol + sulfate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
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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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
(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
-
-
?
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
?
-
-
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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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibited by dithiothreitol and 2-mercaptoethanol
-
additional information
-
addition of EDTA does not eliminate enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 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
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D184N/H185A
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 column chromatography, Mono Q column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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Release 2023.1 (January 2023)
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