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Information on EC 3.1.6.19 - (R)-specific secondary-alkylsulfatase (type III)
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3.1.6.19 (R)-specific secondary-alkylsulfatase (type III)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. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates . The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II).
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pisa1, sec-alkylsulfatase, sulfatase rs2, s3 secondary alkylsulphohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-specific sec-alkylsulfatase
S3 secondary alkylsulphohydrolase
sec-alkylsulfatase
sulfatase RS2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol-forming]
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. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II).
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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
(2R)-1-(4-chlorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
(2R)-1-(4-fluorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
(2R)-octan-2-yl hydrogen sulfate + H2O
(S)-2-octanol + sulfate
-
-
-
?
(2R)-1-(4-chlorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
-
enantiomeric excess of the product: 16%
-
-
?
(2R)-1-(4-chlorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
-
enantiomeric excess of the product: 16%
-
-
?
(2R)-1-(4-fluorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
-
enantiomeric excess of the product: 16%
-
-
?
(2R)-1-(4-fluorophenyl)propan-2-yl sulfate + H2O
(2S)-1-(4-chlorophenyl)propan-2-ol + sulfate
-
enantiomeric excess of the product: 16%
-
-
?
(2R)-nonan-2-yl sulfate + H2O
(2S)-nonan-2-ol + sulfate
-
enantiomeric excess of the product: 65%
-
-
?
(2R)-nonan-2-yl sulfate + H2O
(2S)-nonan-2-ol + sulfate
-
enantiomeric excess of the product: 65%
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
enantioselectivity expressed by E-value is 21. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
enantioselectivity expressed by E-value is 21. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
-
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
-
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
high enantioselectivity (E-value > 200), enantiomeric excess > 99
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provided the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl sulfate and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
high enantioselectivity (E-value > 200), enantiomeric excess > 99
-
-
?
(2R)-octan-2-yl sulfate + H2O
(2S)-octan-2-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provided the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl sulfate and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
high enantioselectivity (E-value > 200), enantiomeric excess of the product: > 99%
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
high enantioselectivity (E-value > 200), enantiomeric excess of the product: > 99%
-
-
?
(2S)-1-phenylpropan-2-yl sulfate + H2O
(2S)-1-phenylpropan-2-ol + sulfate
-
-
-
-
?
(3R)-pentan-3-yl sulfate + H2O
pentan-3-ol + sulfate
-
low activity
-
-
?
(4R)-heptan-4-yl sulfate + H2O
(4S)-heptan-4-ol + sulfate
-
the L-isomer is much more readily hydrolysed than the D-isomer. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom
-
-
?
(4R)-heptan-4-yl sulfate + H2O
(4S)-heptan-4-ol + sulfate
-
the L-isomer is much more readily hydrolysed than the D-isomer. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom
-
-
?
(5R)-nonan-5-yl sulfate + H2O
nonan-5-ol + sulfate
-
the L-isomer is much more readily hydrolysed than the D-isomer. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom
-
-
?
(5R)-nonan-5-yl sulfate + H2O
nonan-5-ol + sulfate
-
the L-isomer is much more readily hydrolysed than the D-isomer. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom
-
-
?
rac-octan-3-yl sulfate + H2O
(3S)-octan-3-ol + sulfate
-
enantioselectivity expressed by E-value is 4.3. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
rac-octan-3-yl sulfate + H2O
(3S)-octan-3-ol + sulfate
-
enantioselectivity expressed by E-value is 4.3. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
rac-octan-3-yl sulfate + H2O
(3S)-octan-3-ol + sulfate
-
enantiomeric excess of the product: 59%
-
-
?
rac-octan-3-yl sulfate + H2O
(3S)-octan-3-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provided the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl sulfate and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
rac-octan-3-yl sulfate + H2O
(3S)-octan-3-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provided the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl sulfate and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
rac-octan-4-yl sulfate + H2O
(4S)-octan-4-ol + sulfate
-
no enantioselectivity is observed, production of racemic 4-octanol. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
rac-octan-4-yl sulfate + H2O
(4S)-octan-4-ol + sulfate
-
no enantioselectivity is observed, production of racemic 4-octanol. The preferred substrates for the enzyme are linear sec-alkyl sulfate esters, particularly 2-, 3-, and 4-octyl sulfates. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom
-
-
?
rac-octan-4-yl sulfate + H2O
(4S)-octan-4-ol + sulfate
-
enantiomeric excess of the product: 55%
-
-
?
rac-octan-4-yl sulfate + H2O
(4S)-octan-4-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provides the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl- and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
rac-octan-4-yl sulfate + H2O
(4S)-octan-4-ol + sulfate
-
hydrolysis of (R)-enantiomers from the racemate provides the corresponding (S)-configured sec-alcohols. Excellent enantioselectivity is observed for octan-2-yl sulfate. When the sulfate ester moiety is gradually moved toward the center of the molecule (octan-3-yl- and octan-4-yl sulfate), the enantioselectivities decreases, which is due to the fact that the alkyl groups flanking the sulfate ester group became similar in size, thus making the chiral recognition process more difficult
-
-
?
additional information
?
-
-
when rather symmetrical molecules, such as 3- or 4-octyl sulfate, are used, the chiral recognition process gets more difficult as the relative sizes of the two alkyl groups adjacent to the stereogenic sulfate ester group become more similar.
-
-
?
additional information
?
-
-
when rather symmetrical molecules, such as 3- or 4-octyl sulfate, are used, the chiral recognition process gets more difficult as the relative sizes of the two alkyl groups adjacent to the stereogenic sulfate ester group become more similar.
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.099
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y, pH not specified in the publication, temperature not specified in the publication
0.115
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250S, pH not specified in the publication, temperature not specified in the publication
0.151
(2R)-octan-2-yl hydrogen sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.24
(2R)-octan-2-yl hydrogen sulfate
mutant H317A, pH not specified in the publication, temperature not specified in the publication
1.5 - 2
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y/F250G, pH not specified in the publication, temperature not specified in the publication
4.28
(2R)-octan-2-yl hydrogen sulfate
mutant F250G, pH not specified in the publication, temperature not specified in the publication
8.42
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250G, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
(2R)-octan-2-yl hydrogen sulfate
mutant H317A, pH not specified in the publication, temperature not specified in the publication
0.018
(2R)-octan-2-yl hydrogen sulfate
mutant Y417H, pH not specified in the publication, temperature not specified in the publication
0.02
(2R)-octan-2-yl hydrogen sulfate
mutant F250G, pH not specified in the publication, temperature not specified in the publication
0.038
(2R)-octan-2-yl hydrogen sulfate
mutant Y417F, pH not specified in the publication, temperature not specified in the publication
0.38
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250G, pH not specified in the publication, temperature not specified in the publication
1.13
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250S, pH not specified in the publication, temperature not specified in the publication
1.4
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y/F250G, pH not specified in the publication, temperature not specified in the publication
1.73
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y, pH not specified in the publication, temperature not specified in the publication
4.37
(2R)-octan-2-yl hydrogen sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.33
octyl sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.005
(2R)-octan-2-yl hydrogen sulfate
mutant F250G, pH not specified in the publication, temperature not specified in the publication
0.014
(2R)-octan-2-yl hydrogen sulfate
mutant H317A, pH not specified in the publication, temperature not specified in the publication
0.046
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250G, pH not specified in the publication, temperature not specified in the publication
0.919
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y/F250G, pH not specified in the publication, temperature not specified in the publication
9.85
(2R)-octan-2-yl hydrogen sulfate
mutant S233F/F250S, pH not specified in the publication, temperature not specified in the publication
17.5
(2R)-octan-2-yl hydrogen sulfate
mutant S233Y, pH not specified in the publication, temperature not specified in the publication
28.9
(2R)-octan-2-yl hydrogen sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
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
2 - 3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.2
-
5.0: about of 40% of maximal activity with nonan-5-yl sulfate, about 80% of maximal activity with heptan-4-yl sulfate. pH 9.2: about 55% of maximal activity with nonan-5-yl sulfate
6.5 - 9
-
pH 6.5: about 55% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
-
20°C: about 50% of maximal activity, 30°C: optimum, 35°C: about 25% of maximal activity, 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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
Pisa1 shows a preference for secondary rather than primary alkyl sulfates, and enantioselectively hydrolyzes the (R)-enantiomer of rac-2-octyl sulfate, yielding (S)-2-octanol with inversion of absolute configuration as a result of C-O bond cleavage. An invariant histidine (His317) near the sulfate-binding site acts as general acid for crucial protonation of the sulfate leaving group
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Pisa1 forms a dimer. Each protomer consists of three domains: the N-terminal, catalytic alphabetabetaalpha sandwich domain, an alpha-helical dimerization domain and an alpha,beta-mixed C-terminal domain. Comparison with the structure of alkyl sulfatase SdsA1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H317A
1300fold decrease in kcat, whereas Km is only slightly increased
S233F/F250G
three-fold to four-fold times lower kcat value and a 10fold higer Km value, variant displays activity towardstowards (S)-2-octyl sulfate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
stereoselctive organic synthesis, stereoselective and enantioselective biohydrolysis of sulfate esters of sec-alcohols
synthesis
-
stereoselective organic synthesis, enantioselective hydrolysis of rac-secondary-alkyl sulphate esters
synthesis
-
stereoselective organic synthesis, enantioselective hydrolysis of rac-secondary-alkyl sulphate esters
-
synthesis
-
stereoselctive organic synthesis, stereoselective and enantioselective biohydrolysis of sulfate esters of sec-alcohols
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pogorevc, M.; Kroutil, W.; Wallner, S.R.; Faber, K.
Enantioselective stereoinversion in the kinetic resolution of rac-sec-alkyl sulfate esters by hydrolysis with an alkylsulfatase from Rhodococcus ruber DSM 44541 furnishes homochiral products
Angew. Chem. Int. Ed. Engl.
41
4052-4954
2002
Rhodococcus ruber, Rhodococcus ruber DSM 44541
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
Shaw, D.J.; Dodgson, K.S.; White, G.F.
Substrate specificity and other properties of the inducible S3 secondary alkylsulphohydrolase purified from the detergent-degrading bacterium Pseudomonas C12B
Biochem. J.
187
181-190
1980
Pseudomonas sp., Pseudomonas sp. C12B
brenda
Gadler, P.; Glueck, S.M.; Kroutil, W.; Nestl, B.M.;, Larissegger-Schnell, B.; Ueberbacher, B.T.; Wallner, S.R.; Faber, K.
Biocatalytic approaches for the quantitative production of single stereoisomers from racemates
Biochem. Soc. Trans.
34
296-300
2006
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Wallner, S.R.; Nestl, B.M.; Faber, K.
Highly enantioselective stereo-inverting sec-alkylsulfatase activity of hyperthermophilic Archaea
Org. Biomol. Chem.
3
2652-2656
2005
Saccharolobus shibatae, Saccharolobus shibatae DSM 5389, Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617, Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Wallner, S.R.; Nestl, B.M.; Faber, K.
Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639
Org. Lett.
6
5009-5010
2004
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Knaus, T.; Schober, M.; Kepplinger, B.; Faccinelli, M.; Pitzer, J.; Faber, K.; Macheroux, P.; Wagner, U.
Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates
FEBS J.
279
4374-4384
2012
Pseudomonas sp. DSM 6611 (F8KAY7)
brenda
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