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(+)-cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
wild type enzyme and mutant enzyme W263F hydrolyze the (+)-enantiomer approximately 3 and 4.5 times faster than the (-)-enantiomer
-
-
?
chlorpyrifos + H2O
O,O-diethylphosphorothioate + 3,5,6-trichloropyridin-2-ol
low activity, cf. EC 3.1.8.2
-
-
?
coumaphos + H2O
O,O-diethylphosphorothioate + 3-chloro-7-hydroxy-4-methyl-2H-chromen-2-one
cf. EC 3.1.8.2
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
fenitrothion + H2O
O,O-diethylphosphorothioate + 3-methyl-4-nitrophenol
-
-
-
?
fensulfothion + H2O
O,O-diethylphosphorothioate + 4-(methylsulfinyl)phenol
some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants
-
-
?
malathion + H2O
?
-
-
-
?
malathion + H2O
O,O-diethylphosphorothioate + diethyl 2-mercaptosuccinate
low activity
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-isopropyl methylphosphonofluoridate + H2O
?
i.e. sarin
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
high activity with enzyme mutant C258L/I261F/W263A
-
-
?
ethyl paraoxon + H2O
?
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
paraoxon is the best substrate for the purified arylesterase
-
-
?
additional information
?
-
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
additional information
?
-
the enzyme possesses phosphotriesterase and a very high lactonase activity, structure-function relationship, overview
-
-
?
additional information
?
-
-
the enzyme possesses phosphotriesterase and a very high lactonase activity, structure-function relationship, overview
-
-
?
additional information
?
-
the phosphotriesterase-like lactonase enzyme is bifunctional showing lactonase (EC 3.1.1.81) and phosphotriesterase (EC 3.1.8.1 and 3.1.8.2) activities
-
-
?
additional information
?
-
substrate docking analysis. The C258 residue in the active site is involved in an interaction with the oxygen atom from the amide in the lactone analogue
-
-
?
additional information
?
-
the enzyme shows lactonase activity with N-(3-oxodecanoyl)-L-homoserine lactone, undecanoic-gamma-lactone, and undecanoic-delta-lactone, cf. EC 3.1.1.81
-
-
?
additional information
?
-
-
the enzyme shows lactonase activity with N-(3-oxodecanoyl)-L-homoserine lactone, undecanoic-gamma-lactone, and undecanoic-delta-lactone, cf. EC 3.1.1.81
-
-
?
additional information
?
-
-
a organophosphate-degrading enzyme
-
-
?
additional information
?
-
-
substrate specificity with organophosphorous compounds, overview
-
-
?
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2-propanol
55% residual activity in the presence of 90% (v/v) 2-propanol, after 60 min at 70°C
acetonitrile
43% residual activity in the presence of 90% (v/v) acetonitrile, after 60 min at 70°C
diethyl dicarbonate
6% residual activity in the presence of 5 mM diethyl dicarbonate, after 30 min at 30°C
diisopropylfluorophosphate
complete inactivation at 5 mM diisopropylfluorophosphate, after 30 min at 30°C
dimethyl sulfoxide
71% residual activity in the presence of 90% (v/v) dimethyl sulfoxide, after 60 min at 70°C
eserine
92% residual activity in the presence of 5 mM eserine, after 30 min at 30°C
ethanol
63% residual activity in the presence of 90% (v/v) ethanol, after 60 min at 70°C
Hg2+
complete inactivation at 5 mM Hg2+, after 30 min at 30°C
methanol
48% residual activity in the presence of 90% (v/v) methanol, after 60 min at 70°C
NaCl
76% residual activity in the presence of 2 M NaCl, after 60 min at 70°C
o-phenanthroline
-
inactivation
p-chloromercuribenzoate
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
petroleum ether
-
petroleum ether slightly reduces the activity down to 78%
-
Phenylglyoxal
97% residual activity in the presence of 5 mM phenylglyoxal, after 30 min at 30°C
phenylmethylsulfonyl fluoride
23% residual activity in the presence of 5 mM phenylmethylsulfonyl fluoride, after 30 min at 30°C
SDS
about half of the activity is retained at 1% SDS after incubation for 60 min at 70°C, the addition of 5% SDS completely eliminates the enzyme activity at 70°C
Toluene
-
toluene slightly reduces the activity down to 74%
Triton X-100
11% residual activity in the presence of 5% (v/v) Tween 80, after 60 min at 70°C
Tween 80
21% residual activity in the presence of 5% (v/v) Tween 80, after 60 min at 70°C
Urea
88% residual activity in the presence of 8 M urea, after 60 min at 70°C
xylene
-
xylene decreases the enzyme activity by more than 75%
fensulfothion
-
fensulfothion
inhibits the wild-type enzyme, while some enzyme mutants are also capable of degrading fensulfothion as substrate
EDTA
-
inactivation
EDTA
92% residual activity in the presence of 10 mM EDTA, after 30 min at 75°C
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commercial soap LM1
wild-type SsoPox, at 70°C, 13fold enhancement of hydrolytic activity in the presence of 0.05% LM1, and for mutant C258L/I261F/W263A at 65°C 1.3fold enhancement
-
sodium deoxycholate
0.05%, approximately 33times catalytic efficiency enhancement compared to that without detergent
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
the enzyme is activated by 87% by incubation with 1% (w/v) 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, at 30°C
dimethyl sulfoxide
21% increase of activity at 50% (v/v) dimethyl sulfoxide, at 30°C
ethanol
15% increase of activity at 50% (v/v) ethanol, at 30°C
Lubrol
the enzyme is activated by 14% by incubation with 1% Lubrol, at 30°C
-
Methylcyclohexane
-
about 250% activity at 100% (v/v)
paraoxon
115 increase of activita in the presence of 0.5 mM paraoxon, after 30 min at 30°C
pyridoxal 5'-phosphate
110% activity in the presence of 5 mM pyridoxal 5'-phosphate, after 30 min at 30°C
Tween 20
the enzyme is activated by 67% by incubation for 60 min with 1% (v/v) Tween 20 at 30°C
SDS
0.01%, approximately 12.5 times catalytic efficiency enhancement compared to that without detergent
SDS
0.1% (w/v), 25°C, wild type enzyme, 11-fold increase of specific activity, activation is stable up to 40 h. The activating effect is reduced at 70°C
SDS
wild-type SsoPox, at 70°C, 17fold enhancement of hydrolytic activity in the presence of 0.025% SDS, and for mutant C258L/I261F/W263A at 65°C 2fold enhancement
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0.107 - 1.586
diethyl-paraoxon
0.16
malathion
25°C, pH 9.0
2.14
methyl paraoxon
25°C, pH 9.0
0.12
methyl parathion
25°C, pH 9.0
0.205 - 0.246
methyl paraoxon
additional information
additional information
-
0.107
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C, with 0.025% SDS
0.325
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C, with 0.025% SDS
0.38
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C
1.586
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C
0.064
paraoxon
pH 8.0, 70°C, wild-type enzyme
0.075
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W
0.153
paraoxon
pH 8.0, 70°C, mutant enzyme W263F
0.272
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/W263F
0.41
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I261F
1.2
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I98F/I261F
2.36
paraoxon
pH 8.0, 70°C
3.27
paraoxon
70°C, pH 9.0
24.25
paraoxon
25°C, pH 9.0
0.205
methyl paraoxon
-
pH 8.0, 70°C, recombinant enzyme
0.246
methyl paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.005
paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.06
paraoxon
-
pH 8.0, 70°C, recombinant enzyme
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis of phosphotriesterase activity
-
additional information
additional information
-
first order kinetics
-
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C258A
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
C258L
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
D141T
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
F46L/C258A/W263M/I280T
site-directed mutagenesis, mutant alphasA6, the mutant shows altered substrate specificity compared to the wild-type enzyme
I767T
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
L130P
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
L228M
site-directed mutagenesis
L72I/Y99F/I122L/L228M/F229S/W263L
site-directed mutagenesis, mutant alphasC6, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/D141T
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
V27A/I76T/Y97W/Y99F/L130P/L226V
site-directed mutagenesis, mutant alphasB5, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263I
site-directed mutagenesis, mutant alphasB5 W263I, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263L
site-directed mutagenesis, mutant alphasB5 W263L, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263M
site-directed mutagenesis, mutant alphasB5 W263M, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/Y97W/L228M/W263M
site-directed mutagenesis, the mutant alphasD6 enzyme demonstrates a large increase in catalytic efficiencies compared to the wild-type enzyme, with increases of 2210fold, 163fold, 58fold, and 16fold against methyl-parathion, malathion, ethyl-paraoxon, and methyl-paraoxon, respectively
V27A/Y97W/Y99F
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
W263I
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263L
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263N
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263Q
kcat/Km for paraoxon is 3.5fold lower than wild-type value
Y97W/I261F
kcat/Km for paraoxon is 1.4fold higher than wild-type value
Y97W/I98F/I261F
kcat/Km for paraoxon is 1.2fold higher than wild-type value
Y97W/W263F
kcat/Km for paraoxon is 1.6fold higher than wild-type value
Y97W/W263Q
kcat/Km for paraoxon is 1.7fold lower than wild-type value
Y99F
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
C105S
mutant shows 24.0% activity compared to the wild type enzyme
C107S
mutant shows 30.8% activity compared to the wild type enzyme
C129S
mutant shows 3.6% activity compared to the wild type enzyme
D251N
mutant shows 0.6% activity compared to the wild type enzyme
H281N
mutant shows 19.4% activity compared to the wild type enzyme
S156A
mutant shows 0.012% activity compared to the wild type enzyme
W263I
-
the mutant has increased lactonase and phosphotriesterase activities compared to the wild type
C258L/I261F/W263A
site-directed mutagenesis, in vitro evolution, the mutant activity is promiscuous. The combination of C258L, I261F, and W263A mutations in the SsoPox triple mutant improves the hydrolytic specific activity in terms of kcat/KM toward paraoxon 12fold, the kcat 294fold compared to wild-type SsoPox, while the KM value increases
C258L/I261F/W263A
site-directed mutagenesis, mutant alphasA1, the mutant shows altered substrate specificity compared to the wild-type enzyme
C258L/I261F/W263A
site-directed mutagenesis, mutant SsoPox 3 M
V27A
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
W263F
kcat/Km for paraoxon is 6.5fold higher than wild-type value
W263F
mutant is able to convert paraoxon to 4-nitrophenol
W263F
site-directed mutagenesis, the W263 residue is previously demonstrated to be involved in the formation of an hydrophobic channel for the substrate leaving group, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
Y97W
site-directed mutagenesis
Y97W
kcat/Km for paraoxon is 2.4fold higher than wild-type value
additional information
evolution of a lactonase into a phosphotriesterase, semi-rational engineering approach is used to design an efficient and thermostable organophosphate hydrolase, starting from enzyme SsoPox from Sulfolobus solfataricus as a lactonase scaffold. In particular, by in vitro evolution of the SsoPox ancillary promiscuous activity, the triple mutant C258L/I261F/W263A is obtained which, retaining its inherent stability, shows an enhancement of its hydrolytic activity on paraoxon up to 300fold. The mutant is tested in formulations of different solvents (methanol or ethanol) or detergents (SDS or a commercial soap) for the cleaning of pesticide-contaminated surfaces. Construction of a chimeric gene ssopox-pte by insertion of 16 conserved residues of pte gene in the ssopox sequence. Recombination by DNA StEP between ssopox-pte chimera and ssopox gene
additional information
optimization of enzyme production scale-up for establishment of an industrial purification process using SsoPox C258L/I261F/W263A mutant enzyme SsoPox 3 M, set up of high cell density fermentation strategies
additional information
the lactonase SsoPox is engineered for higher phosphotriesterase activity using structure-based combinatorial libraries. By comparing structures of enzymes with similar topology, it is possible to redesign, using modelling tools, the active site cavity of SsoPox to mimic as closely as possible that of enzyme BdPTE from Brevundimonas diminuta. Some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. Structure-based identification of mutations, structure-activity analysis of wild-type and mutant enzymes, overview. Construction of SsoPox monovariants alphasA1, alphasA6, alphasB5, alphasC6 and alphasD6
additional information
-
the lactonase SsoPox is engineered for higher phosphotriesterase activity using structure-based combinatorial libraries. By comparing structures of enzymes with similar topology, it is possible to redesign, using modelling tools, the active site cavity of SsoPox to mimic as closely as possible that of enzyme BdPTE from Brevundimonas diminuta. Some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. Structure-based identification of mutations, structure-activity analysis of wild-type and mutant enzymes, overview. Construction of SsoPox monovariants alphasA1, alphasA6, alphasB5, alphasC6 and alphasD6
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106
estimated denaturation temperature
65
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 6.6 h, completely stable
75
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, loss of 10% activity after 6.6 h
85
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, loss of 30% activity after 6.6 h, t1/2 is 5.8 h
90
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, loss of 40% activity after 5.0 h, t1/2 is 2.2 h
95
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, loss of 40% activity after 1.5 h, t1/2 is 25 min
100
-
purified recombinant enzyme, half-life is 90 min
50 - 94
the enzyme retains 52% of its activity after 50 h of incubation at 90°C, the enzyme is rapidly inactivated above 94°C, most of the enzyme activity is maintained for 5 days at 50°C, the enzyme activity gradually decreases with time at higher temperatures, approximately 70% of the enzyme activity remains after 5 days at 70°C, and 52% of it is still preserved after 50 h at 90°C, however, at 90°C after 5 days, the enzyme is completely inactivated
70 - 85
-
purified recombinant enzyme, 4 h, completely stable
95
-
purified recombinant enzyme, half-life is 4 h
additional information
highly thermostable enzyme
additional information
-
highly thermostable enzyme
additional information
-
106°C is the melting temperature. The temperatures required to lose one half of enzymatic activity in 5 minutes are 92°C and 130°C in liquid and solid states, respectively. More than 30% activity remains after autoclaving the enzyme powder at 121°C for 15 min
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Elias, M.; Dupuy, J.; Merone, L.; Lecomte, C.; Rossi, M.; Masson, P.; Manco, G.; Chabriere, E.
Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase
Acta Crystallogr. Sect. F
63
553-555
2007
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
brenda
Merone, L.; Mandrich, L.; Rossi, M.; Manco, G.
A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties
Extremophiles
9
297-305
2005
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
brenda
Park, Y.J.; Yoon, S.J.; Lee, H.B.
A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression
J. Bacteriol.
190
8086-8095
2008
Saccharolobus solfataricus (B5BLW5), Saccharolobus solfataricus P1 (B5BLW5)
brenda
Elias, M.; Dupuy, J.; Merone, L.; Mandrich, L.; Porzio, E.; Moniot, S.; Rochu, D.; Lecomte, C.; Rossi, M.; Masson, P.; Manco, G.; Chabriere, E.
Structural basis for natural lactonase and promiscuous phosphotriesterase activities
J. Mol. Biol.
379
1017-1028
2008
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus
brenda
Del Vecchio, P.; Elias, M.; Merone, L.; Graziano, G.; Dupuy, J.; Mandrich, L.; Carullo, P.; Fournier, B.; Rochu, D.; Rossi, M.; Masson, P.; Chabriere, E.; Manco, G.
Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus
Extremophiles
13
461-470
2009
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VT7)
brenda
Ng, F.S.; Wright, D.M.; Seah, S.Y.
Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing
Appl. Environ. Microbiol.
77
1181-1186
2010
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VT7)
brenda
Merone, L.; Mandrich, L.; Porzio, E.; Rossi, M.; Mller, S.; Reiter, G.; Worek, F.; Manco, G.
Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase
Bioresour. Technol.
101
9204-9212
2010
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VT7)
brenda
Mandrich, L.; Merone, L.; Manco, G.
Hyperthermophilic phosphotriesterases/lactonases for the environment and human health
Environ. Technol.
31
1115-1127
2010
Sulfolobus acidocaldarius, Saccharolobus solfataricus
brenda
Hiblot, J.; Gotthard, G.; Chabriere, E.; Elias, M.
Characterisation of the organophosphate hydrolase catalytic activity of SsoPox
Sci. Rep.
2
779
2012
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VT7)
brenda
Restaino, O.F.; Borzacchiello, M.G.; Scognamiglio, I.; Porzio, E.; Manco, G., Fedele, L., Donatiello, C., De Rosa, M.; Schiraldi, C.
Boosted large-scale production and purification of a thermostable archaeal phosphotriesterase-like lactonase for organophosphate decontamination
J. Ind. Microbiol. Biotechnol.
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363-375
2017
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (Q97VT7)
brenda
Del Giudice, I.; Coppolecchia, R.; Merone, L.; Porzio, E.; Carusone, T.M.; Mandrich, L.; Worek, F.; Manco, G.
An efficient thermostable organophosphate hydrolase and its application in pesticide decontamination
Biotechnol. Bioeng.
113
724-734
2016
Saccharolobus solfataricus (Q97VT7)
brenda
Restaino, O.F.; Borzacchiello, M.G.; Scognamiglio, I.; Fedele, L.; Alfano, A.; Porzio, E.; Manco, G.; De Rosa, M.; Schiraldi, C.
High yield production and purification of two recombinant thermostable phosphotriesterase-like lactonases from Sulfolobus acidocaldarius and Sulfolobus solfataricus useful as bioremediation tools and bioscavengers
BMC Biotechnol.
18
18
2018
Sulfolobus acidocaldarius, Saccharolobus solfataricus (Q97VT7)
brenda
Remy, B.; Plener, L.; Poirier, L.; Elias, M.; Daude, D.; Chabriere, E.
Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications
Sci. Rep.
6
37780
2016
Saccharolobus solfataricus
brenda
Jacquet, P.; Hiblot, J.; Daude, D.; Bergonzi, C.; Gotthard, G.; Armstrong, N.; Chabriere, E.; Elias, M.
Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase
Sci. Rep.
7
16745
2017
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus
brenda