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1-naphthyl acetate + H2O
1-naphthol + acetate
2-nitrophenyl dimethylcarbamate + H2O
? + methylamine + CO2
-
-
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
?
3,5-dimethylphenyl N-methylcarbamate + H2O
? + methylamine + CO2
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
aldicarb + H2O
? + methylamine + CO2
an N-methyl carbamate ester + H2O
an alcohol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
carbofuran + H2O
2,3-dihydro-2,2-dimethyl-7-benzofuranol + methylamine + CO2
-
i.e. 2,3-dihydro-2,2-dimethyl-7-benzofuranyl N-methylcarbamate
-
-
?
carbofuran + H2O
7-phenol + methylamine + CO2
carbofuran + H2O
? + methylamine + CO2
carbofuran + H2O
carbofuran phenol + methylamine + CO2
dimethyl umbelliferyl phosphate + H2O
umbelliferone + dimethyl phosphate
-
-
-
-
?
fenobucarb + H2O
? + methylamine + CO2
iprovalicarb + H2O
? + methylamine + CO2
-
-
-
?
isoprocarb + H2O
? + methylamine + CO2
methomyl + H2O
methyl (1E)-N-hydroxyethanimidothioate + methylamine + CO2
methylparathion + H2O
?
i.e. O,O-dimethyl-O-4-nitrophenylthiophosphate
-
-
?
metolcarb + H2O
? + methylamine + CO2
oxamyl + H2O
? + methylamine + CO2
oxamyl oxime + H2O
? + methylamine + CO2
-
-
-
?
pirimicarb + H2O
? + methylamine + CO2
-
-
-
?
propoxur + H2O
? + methylamine + CO2
prosulfocarb + H2O
? + methylamine + CO2
-
-
-
?
xylylcarb + H2O
? + methylamine + CO2
additional information
?
-
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
51% activity compared to carbaryl
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
73% activity compared to carbaryl
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
73% activity compared to carbaryl
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
Blastobacter sp. M501
-
2% activity compared to carbaryl
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
?
Blastobacter sp. M501
-
66% activity compared to carbaryl
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
?
XMC, 115% activity compared to carbaryl
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
? + methylamine + CO2
-
43% activity compared to carbaryl
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
? + methylamine + CO2
-
91% activity compared to carbaryl
-
-
?
3,5-dimethylphenyl N-methylcarbamate + H2O
? + methylamine + CO2
-
91% activity compared to carbaryl
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
80% activity compared to carbaryl
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
77% activity compared to carbaryl
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
77% activity compared to carbaryl
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Blastobacter sp. M501
-
4% activity compared to carbaryl
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
acetamide + H2O
?
-
-
-
-
?
acetamide + H2O
?
-
-
-
-
?
aldicarb + H2O
?
-
34.74% activity compared to carbaryl
-
-
?
aldicarb + H2O
?
-
-
-
-
?
aldicarb + H2O
?
low activity
-
-
?
aldicarb + H2O
?
-
-
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
-
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
i.e. 2-methyl-2-(methylthio)propionaldehyde O-(N-methylcarbamoyl)oxime
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
18% activity compared to carbaryl
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
lowest activity
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
i.e. 2-methyl-2-(methylthio)propionaldehyde O-(methylcarbamoyl)oxime
-
-
?
aldicarb + H2O
? + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
preferred substrate, 100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
preferred substrate, 100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
Blastobacter sp. M501
-
i.e. 1-naphthyl N-methylcarbamate, 100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
highest activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
i.e. 1-naphthyl N-methylcarbamate
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
best substrate
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
i.e. 1-naphthyl N-methylcarbamate, 100% activity
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbaryl + H2O
1-naphthol + methylamine + CO2
-
-
-
-
?
carbofuran + H2O
7-phenol + methylamine + CO2
-
51.24% activity compared to carbaryl
-
-
?
carbofuran + H2O
7-phenol + methylamine + CO2
-
-
-
-
?
carbofuran + H2O
?
-
-
-
?
carbofuran + H2O
?
-
-
-
-
?
carbofuran + H2O
?
-
-
-
?
carbofuran + H2O
?
-
-
-
?
carbofuran + H2O
?
-
-
-
?
carbofuran + H2O
?
-
-
-
-
?
carbofuran + H2O
? + methylamine + CO2
-
-
-
-
?
carbofuran + H2O
? + methylamine + CO2
-
i.e. 2,3-dihydro-2,2-dimethyl-7-benzofuranyl N-methylcarbamate
-
-
?
carbofuran + H2O
carbofuran phenol + methylamine + CO2
-
83% activity compared to carbaryl
-
-
?
carbofuran + H2O
carbofuran phenol + methylamine + CO2
-
the extent of hydrolysis of carbofuran is about 0.6fold compared to carbaryl
-
-
?
carbofuran + H2O
carbofuran phenol + methylamine + CO2
-
-
-
-
?
carbofuran + H2O
carbofuran phenol + methylamine + CO2
-
-
-
-
?
carbofuran + H2O
carbofuran phenol + methylamine + CO2
-
-
-
?
fenobucarb + H2O
?
-
69.84% activity compared to carbaryl
-
-
?
fenobucarb + H2O
?
Blastobacter sp. M501
-
i.e 2-S-butylphenyl N-methylcarbamate, 2% activity compared to carbaryl
-
-
?
fenobucarb + H2O
?
-
-
-
?
fenobucarb + H2O
?
i.e 2-s-butylphenyl N-methylcarbamate, 11% activity compared to carbaryl
-
-
?
fenobucarb + H2O
? + methylamine + CO2
-
32% activity compared to carbaryl
-
-
?
fenobucarb + H2O
? + methylamine + CO2
-
-
-
-
?
formamide + H2O
?
-
-
-
-
?
formamide + H2O
?
-
-
-
-
?
isoprocarb + H2O
?
-
i.e. 2-isopropylphenyl N-methylcarbamate, 2% activity compared to carbaryl
-
-
?
isoprocarb + H2O
?
Blastobacter sp. M501
-
i.e. 2-isopropylphenyl N-methylcarbamate, 2% activity compared to carbaryl
-
-
?
isoprocarb + H2O
?
-
-
-
?
isoprocarb + H2O
?
-
-
-
-
?
isoprocarb + H2O
?
-
-
-
?
isoprocarb + H2O
?
-
-
-
?
isoprocarb + H2O
?
i.e. 2-isopropylphenyl N-methylcarbamate, 21% activity compared to carbaryl
-
-
?
isoprocarb + H2O
?
-
-
-
?
isoprocarb + H2O
?
-
-
-
-
?
isoprocarb + H2O
? + methylamine + CO2
-
43% activity compared to carbaryl
-
-
?
isoprocarb + H2O
? + methylamine + CO2
-
the extent of hydrolysis of carbofuran is about 0.5fold compared to carbaryl
-
-
?
isoprocarb + H2O
? + methylamine + CO2
-
-
-
-
?
methomyl + H2O
methyl (1E)-N-hydroxyethanimidothioate + methylamine + CO2
-
-
-
-
?
methomyl + H2O
methyl (1E)-N-hydroxyethanimidothioate + methylamine + CO2
-
-
-
-
?
metolcarb + H2O
?
Blastobacter sp. M501
-
i.e. 3-methylphenyl N-methylcarbamate, 62% activity compared to carbaryl
-
-
?
metolcarb + H2O
?
i.e. 3-methylphenyl N-methylcarbamate, 54% activity compared to carbaryl
-
-
?
metolcarb + H2O
? + methylamine + CO2
-
304% activity compared to carbaryl
-
-
?
metolcarb + H2O
? + methylamine + CO2
-
87% activity compared to carbaryl
-
-
?
metolcarb + H2O
? + methylamine + CO2
-
-
-
-
?
oxamyl + H2O
?
-
31.25% activity compared to carbaryl
-
-
?
oxamyl + H2O
? + methylamine + CO2
-
low activity
-
-
?
oxamyl + H2O
? + methylamine + CO2
-
-
-
-
?
oxamyl + H2O
? + methylamine + CO2
-
-
-
?
propoxur + H2O
?
-
66.01% activity compared to carbaryl
-
-
?
propoxur + H2O
?
Blastobacter sp. M501
-
i.e. 2-isopropoxyphenyl N-methylcarbamate, 14% activity compared to carbaryl
-
-
?
propoxur + H2O
?
-
-
-
-
?
propoxur + H2O
?
i.e. 2-isopropoxyphenyl N-methylcarbamate, 9% activity compared to carbaryl
-
-
?
propoxur + H2O
?
-
-
-
-
?
propoxur + H2O
? + methylamine + CO2
-
54% activity compared to carbaryl
-
-
?
propoxur + H2O
? + methylamine + CO2
-
-
-
-
?
propoxur + H2O
? + methylamine + CO2
-
-
-
-
?
xylylcarb + H2O
?
Blastobacter sp. M501
-
i.e. 3,4-dimethylphenyl N-methylcarbamate, 88% activity compared to carbaryl
-
-
?
xylylcarb + H2O
?
i.e. 3,4-dimethylphenyl N-methylcarbamate, 61% activity compared to carbaryl
-
-
?
xylylcarb + H2O
? + methylamine + CO2
-
66% activity compared to carbaryl
-
-
?
xylylcarb + H2O
? + methylamine + CO2
-
93% activity compared to carbaryl
-
-
?
additional information
?
-
-
no activity with diethyl umbelliferyl phosphate, chlorpyrifos and parathion
-
-
-
additional information
?
-
-
the enzyme is unable to hydrolyze parathion (O,O-diethyl O-(4-nitrophenyl) phosphorothioate), S-ethyl dipropylthiocarbamate, or chlorpropham (isopropyl 3-chlorocarbanilate)
-
-
-
additional information
?
-
-
the purified enzyme has no urease activity
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze N-acetyl-4-aminophenol or methomyl
-
-
-
additional information
?
-
-
the enzyme shows no catalytic activity on any carbamate pesticide other than methomyl, including carbaryl, isoprocarb, fenobucarb, propoxur, aldicarb, carbofuran, and oxamyl
-
-
-
additional information
?
-
-
the enzyme shows no catalytic activity on any carbamate pesticide other than methomyl, including carbaryl, isoprocarb, fenobucarb, propoxur, aldicarb, carbofuran, and oxamyl
-
-
-
additional information
?
-
-
the enzyme is not able to hydrolyze chloropropham, fenobucarb, propoxur, and isoprocarb
-
-
-
additional information
?
-
-
hydrolase activity is undetectable with chloropropham, S-ethyl dipropylthiocarbamate, and parathion
-
-
-
additional information
?
-
-
hydrolase activity is undetectable with chloropropham, S-ethyl dipropylthiocarbamate, and parathion
-
-
-
additional information
?
-
Blastobacter sp. M501
-
hydrolase activity is not detected with the substrates of fenitrothion, methylparathion, paraoxon, chloropropham, swep, propanil, and linuron
-
-
-
additional information
?
-
-
no activity with carbofuran and aldicarb
-
-
-
additional information
?
-
-
the purified enzyme does not hydrolyze 2-nitrophenyl dimethylcarbamate
-
-
-
additional information
?
-
-
no activity with isopropyl 3-chlorocarbanilate, S-ethyl N,N-dipropylthiocarbamate, and 2-nitrophenyldimethylcarbamate
-
-
-
additional information
?
-
the enzyme cannot hydrolyze N-acetyl 4-aminophenol, methomyl and oxamyl
-
-
-
additional information
?
-
hydrolase activity is undetectable with the substrates of carbofuran and chloropropham
-
-
-
additional information
?
-
-
no activity with methomyl
-
-
-
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2-chloromercuribenzoate
-
21% residual activity at 1 mM
-
2-mercaptoethanol
-
the enzyme shows 10% activity in the presence of 0.1% (v/v) 2-mercaptoethanol. Higher concentrations completely inactivate the enzyme. However, the activity of the enzyme is recovered when 2-mercaptoethanol was removed by dialysis
acetone
-
20% residual activity in 25% (v/v) acetone
acetonitrile
-
20% residual activity in 14% (v/v) acetonitrile
Ag+
-
complete inhibition at 1 mM
diisopropylfluorophosphate
dithiothreitol
-
the enzyme shows 10% activity in the presence of 0.1% (v/v) dithiothreitol. Higher concentrations completely inactivate the enzyme
Fe2+
-
complete inhibition at 1 mM
iodoacetic acid
-
13% residual activity at 1 mM
methanol
-
20% residual activity in 25% (v/v) methanol
Mg2+
-
93% residual activity at 1 mM
Mn2+
-
96% residual activity at 1 mM
paraoxon
-
less than 1% residual activity at 1 mM
Phenanthroline
-
complete inhibition at 10 mM
phenylmethylsulfonyl fluoride
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
90% residual activity at 1 mM
Cu2+
-
91% residual activity at 1 mM
Cu2+
41.08% residual activity at 1 mM
diisopropylfluorophosphate
-
37% residual activity at 1 mM
diisopropylfluorophosphate
-
33.6% residual activity at 1 mM
EDTA
-
the addition of EDTA results in the complete inactivation of the enzyme. Addition of 1 mM Mn2+ to the reaction mixture restores the activity to 70% of its original level
EDTA
-
about 40% inhibition at 100 mM
EDTA
-
strongly inhibited by 1 mM EDTA. The activity can be restored after supplementing with Mn2+, Co2+, Mg2+, Ca2+ and Ni2+
Fe3+
-
complete inhibition at 1 mM
Hg2+
-
20% residual activity at 1 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
Blastobacter sp. M501
-
complete inhibition at 1 mM
Hg2+
37.67% residual activity at 1 mM
Hg2+
the enzyme is completely inhibited by 1 mM Hg2+
phenylmethylsulfonyl fluoride
-
less than 4% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
24.6% residual activity at 1 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
95% residual activity at 1 mM
additional information
-
not inhibited by EDTA, N-ethylmaleimide and iodoacetamide
-
additional information
-
not inhibited by EDTA and phenanthroline
-
additional information
Blastobacter sp. M501
-
EDTA, iodoacetoamide, diisopropyl fluorophosphate, and paraoxon have no effect on the enzyme activity
-
additional information
-
EDTA does not affect the enzyme activity
-
additional information
EDTA has no effect on the enzyme activity
-
additional information
EDTA, iodoacetamide, diisopropyl fluorophosphate, and paraoxon have no effect on the enzyme activity
-
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D191A
-
the activity of the mutant enzyme is completely abolished
E207A
-
the activity of the mutant enzyme is completely abolished
G162A
-
the activity of the mutant enzyme is completely abolished
H193A
-
the mutant retains 10% of hydrolysis activity against methomyl as compared to the wild type enzyme
N164A
-
the activity of the mutant enzyme is completely abolished
D191A
-
the activity of the mutant enzyme is completely abolished
-
E207A
-
the activity of the mutant enzyme is completely abolished
-
G162A
-
the activity of the mutant enzyme is completely abolished
-
H193A
-
the mutant retains 10% of hydrolysis activity against methomyl as compared to the wild type enzyme
-
N164A
-
the activity of the mutant enzyme is completely abolished
-
F152L
the mutation determines the catalytic preference for bicyclic carbamate substrates (carbofuran, carbaryl)
L152F
-
the mutation renders the enzyme completely inactive against carbofuran
T494A
the mutation determines the preference for monocyclic carbamate substrates (isoprocarb, propoxur)
T570I
the mutation determines the preference for linear carbamate substrates (oxamyl, aldicarb)
F152L
-
the mutation determines the catalytic preference for bicyclic carbamate substrates (carbofuran, carbaryl)
T494A
-
the mutation determines the preference for monocyclic carbamate substrates (isoprocarb, propoxur)
T570I
-
the mutation determines the preference for linear carbamate substrates (oxamyl, aldicarb)
H451A
the mutant shows wild type activity
H464A
the mutant shows wild type activity
H467A
the mutant shows 32.68% activity compared to the wild type enzyme
H467A/H477A
the mutant shows 7.28% activity compared to the wild type enzyme
H477A
the mutant shows 78.28% activity compared to the wild type enzyme
H504A
the mutant shows 1.34% activity compared to the wild type enzyme
F152L
the mutation determines the catalytic preference for bicyclic carbamate substrates (carbofuran, carbaryl)
T494A
the mutation determines the preference for monocyclic carbamate substrates (isoprocarb, propoxur)
T570I
the mutation determines the preference for linear carbamate substrates (oxamyl, aldicarb)
F152L
the mutation determines the catalytic preference for bicyclic carbamate substrates (carbofuran, carbaryl)
H351A
-
the mutant loses hydrolysis activity against carbofuran
H353A
-
the mutant loses hydrolysis activity against carbofuran
H453A
-
the mutant loses hydrolysis activity against carbofuran
H495A
-
the mutant loses hydrolysis activity against carbofuran
T494A
the mutation determines the preference for monocyclic carbamate substrates (isoprocarb, propoxur)
T570I
the mutation determines the preference for linear carbamate substrates (oxamyl, aldicarb)
F152L
-
the mutation determines the catalytic preference for bicyclic carbamate substrates (carbofuran, carbaryl)
T494A
-
the mutation determines the preference for monocyclic carbamate substrates (isoprocarb, propoxur)
T570I
-
the mutation determines the preference for linear carbamate substrates (oxamyl, aldicarb)
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-20 or -70°C, purified enzyme in 10 mM K2HPO4 (pH 7.5) in the presence of 20% (v/v) glycerol, 1 month, no loss of activity
-
-70°C, purified enzyme in the presence of 20% (v/v) glycerol, 1 month, no loss of activity
-
-80°C, crude extract and purified enzyme, more than 1 month, no loss of activity
-
0°C, purified enzyme, 48 h, no loss of activity
-
25°C, purified enzyme, 10 days, 10% loss of activity
-
25°C, purified enzyme, 12 h, 15% loss of activity
-
25°C, purified enzyme, 25 days, 47% loss of activity
-
25°C, purified enzyme, 7 days, no loss of activity
-
4°C, after partial purification by DEAE column chromatography, more than 1 month, no loss of activity
-
4°C, crude extract, 24 h, 30% loss of activity
-
4°C, purified enzyme in 10 mM K2HPO4 (pH 7.5), 1 month, 25% loss of activity
-
4°C, purified enzyme in 10 mM K2HPO4 (pH 7.5), 1 week, no loss of activity
-
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ammonium sulfate precipitation, Q Sepharose column chromatography, SP Sepharose column chromatography, and Sephacryl S-200 gel filtration
DEAE column chromatography, TSK phenyl column chromatography and 300SW gel filtration
-
DEAE-cellulose column chromatography, hydroxylapatite column chromatography, and Sephacryl S-300 gel filtration
-
DEAE-cellulose column chromatography, Sephadex G-200 gel filtration, and Macro-prep tert-butyl column chromatography
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His-bind resin column chromatography
His-Spin Protein Miniprep kit
-
Ni-NTA agarose resin column chromatography
Ni-NTA agarose resin column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography
-
Ni-NTA resin column chromatography and Superdex-200 gel filtration
-
phenyl Sepharose column chromatography and Superdex 200 gel filtration
-
protamine sulfate precipitation, ammonium sulfate precipitation, phenyl Sepharose column chromatography, and Biogel A0.5m gel filtration
-
protamine sulfate precipitation, ammonium sulfate precipitation, phenyl Sepharose column chromatography, DEAE-Sepharose column chromatography, and Sephacryl 200 gel filtration
-
protamine sulfate treatment, ammonium sulfate precipitation, phenyl Sepharose column chromatography, DEAE-Sepharose column chromatography, and Superdex 200 gel filtration
-
protamine sulfate treatment, ammonium sulfate precipitation, Phenyl-Sepharose CL-4B column chromatography, DEAE-Toyopearl 650 column chromatography, Toyopearl HW-55 gel filtration, and hydroxylapatite column chromatography
Blastobacter sp. M501
-
Q-Sepharose column chromatography, Sepharose CL-4B column chromatography, hydroxyapatite column chromatography and Sephacryl S-200HR gel filtration
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Q-Sepharose column chromatography, Sepharose CL-4B column chromatography, hydroxyapatite column chromatography and Sephacryl S-200HR gel filtration, and Ni-NTA column chromatography
TSK-DEAE column chromatography, TSK-phenyl column chromatography, and Bio-Gel A0.5m gel filtration
-
Ni-NTA agarose resin column chromatography
Ni-NTA agarose resin column chromatography
Ni-NTA agarose resin column chromatography
Ni-NTA agarose resin column chromatography
-
Ni-NTA agarose resin column chromatography
-
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Mulbry, W.W.; Eaton, R.W.
Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK
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57
3679-3682
1991
Pseudomonas sp. CRL-OK
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Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501
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Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100
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Rhizobium sp. AC100 (Q8RR61)
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Hydrolase CehA and monooxygenase CfdC are responsible for carbofuran degradation in Sphingomonas sp. strain CDS-1
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Sphingomonas sp. CDS-1
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Compartmentalization of the carbaryl degradation pathway Molecular characterization of inducible periplasmic carbaryl hydrolase from Pseudomonas spp.
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Pseudomonas sp. C7, Pseudomonas sp. C5pp (A0A140DCH5)
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Jiang, W.; Zhang, C.; Gao, Q.; Zhang, M.; Qiu, J.; Yan, X.; Hong, Q.
Carbamate C-N hydrolase gene ameH responsible for the detoxification step of methomyl degradation in Aminobacter aminovorans strain MDW-2
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Aminobacter aminovorans, Aminobacter aminovorans MDW-2
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Chaudhry, G.R.; Mateen, A.; Kaskar, B.; Bloda, M.; Riazuddin, S.
Purification and biochemical characterization of the carbamate hydrolase from Pseudomonas sp. 50432
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36
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Pseudomonas sp. 50432
brenda
Jiang, W.; Gao, Q.; Zhang, L.; Wang, H.; Zhang, M.; Liu, X.; Zhou, Y.; Ke, Z.; Wu, C.; Qiu, J.; Hong, Q.
Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1
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189
109938
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Sphingobium sp. CFD-1
brenda
Ke, Z.; Zhu, Q.; Jiang, W.; Zhou, Y.; Zhang, M.; Jiang, M.; Hong, Q.
Heterologous expression and exploration of the enzymatic properties of the carbaryl hydrolase CarH from a newly isolated carbaryl-degrading strain
Ecotoxicol. Environ. Saf.
224
112666
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Agrobacterium sp. XWY-2
brenda
Oeztuerk, B.; Ghequire, M.; Nguyen, T.P.; De Mot, R.; Wattiez, R.; Springael, D.
Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene
Environ. Microbiol.
18
4878-4887
2016
Novosphingobium sp. KN65.2
brenda
Rousidou, C.; Karaiskos, D.; Myti, D.; Karanasios, E.; Karas, P.A.; Tourna, M.; Tzortzakakis, E.A.; Karpouzas, D.G.
Distribution and function of carbamate hydrolase genes cehA and mcd in soils the distinct role of soil pH
FEMS Microbiol. Ecol.
93
fiw219
2017
uncultured bacterium (A0A1L3HJ42), uncultured bacterium (A0A1L3HJ65)
brenda
Hayatsu, M.; Mizutani, A.; Hashimoto, M.; Sato, K.; Hayano, K.
Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100
FEMS Microbiol. Lett.
201
99-103
2001
Arthrobacter sp. RC100
brenda
Zhang, Q.; Liu, Y.; Liu, Y.H.
Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168
FEMS Microbiol. Lett.
228
39-44
2003
Aspergillus niger, Aspergillus niger PY168
brenda
Derbyshire, M.; Karns, J.; Kearney, P.; Nelson, J.
Purification and characterization of an N-methylcarbamate pesticide hydrolyzing enzyme
J. Agric. Food Chem.
35
871-877
1987
Achromobacter sp. WM111
-
brenda
Karns, J.; Tomasek, P.
Carbofuran hydrolase - Purification and properties
J. Agric. Food Chem.
39
1004-1008
1991
Achromobacter sp. WM111
-
brenda
Zhou, Y.; Ke, Z.; Ye, H.; Hong, M.; Xu, Y.; Zhang, M.; Jiang, W.; Hong, Q.
Hydrolase CehA and a novel two-component 1-naphthol hydroxylase CehC1C2 are responsible for the two initial steps of carbaryl degradation in Rhizobium sp. X9
J. Agric. Food Chem.
68
14739-14747
2020
Rhizobium sp. X9
brenda
Tomasek, P.H.; Karns, J.S.
Cloning of a carbofuran hydrolase gene from Achromobacter sp. strain WM111 and its expression in gram-negative bacteria
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171
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Achromobacter sp. WM111
brenda
Chapalmadugu, S.; Chaudhry, G.R.
Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa
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175
6711-6716
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Pseudomonas aeruginosa
brenda
Naqvi, T.; Cheesman, M.J.; Williams, M.R.; Campbell, P.M.; Ahmed, S.; Russell, R.J.; Scott, C.; Oakeshott, J.G.
Heterologous expression of the methyl carbamate-degrading hydrolase MCD
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144
89-95
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Achromobacter sp. WM111
brenda
Zhu, S.; Qiu, J.; Wang, H.; Wang, X.; Jin, W.; Zhang, Y.; Zhang, C.; Hu, G.; He, J.; Hong, Q.
Cloning and expression of the carbaryl hydrolase gene mcbA and the identification of a key amino acid necessary for carbaryl hydrolysis
J. Hazard. Mater.
344
1126-1135
2018
Pseudomonas sp. XWY-1 (A0A1S6TLL2)
brenda
Jiang, W.; Liu, Y.; Ke, Z.; Zhang, L.; Zhang, M.; Zhou, Y.; Wang, H.; Wu, C.; Qiu, J.; Hong, Q.
Substrate preference of carbamate hydrolase CehA reveals its environmental behavior
J. Hazard. Mater.
403
123677
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Sphingomonas sp. CDS-1, Pseudomonas sp. OXA20, Novosphingobium sp. KN65.2 (A0A158SQ52), Sphingobium sp. CFD-1 (A0A6B9IL91), Rhizobium sp. AC100 (Q8RR61)
brenda
Yang, C.; Xu, X.; Liu, Y.; Jiang, H.; Wu, Y.; Xu, P.; Liu, R.
Simultaneous hydrolysis of carbaryl and chlorpyrifos by Stenotrophomonas sp. strain YC-1 with surface-displayed carbaryl hydrolase
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Rhizobium sp. AC100 (Q8RR61)
brenda