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(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
2-naphthyl acetate + H2O
2-naphthol + acetate
4-methyl-2-oxo-2H-chromen-7-yl (2E)-but-2-enoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3,3-dimethylbutanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-cyclopentylpropanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbut-2-enoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbutanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-phenoxybutanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl acetate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl butyrate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl cyclopentanecarboxylate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl heptanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl hexanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl pentanoate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl pivalate + H2O
?
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl propionate + H2O
?
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
4-nitrophenyl thioacetate + H2O
4-nitrophenol + thioacetate
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
alpha-naphthyl butyrate + H2O
alpha-naphthol + butyrate
-
-
-
-
?
alpha-naphthyl propionate + H2O
alpha-naphthol + propionate
-
-
-
-
?
beta-naphthyl acetate + H2O
beta-naphthol + acetate
-
-
-
?
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O
[[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoic acid
carboxyfluorescein diacetate + H2O
carboxyfluorescein + acetate
-
-
-
?
fluorescein diacetate + H2O
?
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O
fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O
fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate
fluorescein-3',6'-bis(oxy)methylene bis(methoxyacetate) + H2O
fluorescein-3'-oxymethyl methoxyacetate + methoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(propoxyacetate) + H2O
fluorescein-3'-oxymethyl propoxyacetate + propoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis[(methylsulfanyl)acetate] + H2O
fluorescein-3'-oxymethyl (methylsulfanyl)acetate + (methylsulfanyl)acetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis[[(propan-2-yl)sulfanyl]acetate] + H2O
fluorescein-3'-oxymethyl [(propan-2-yl)sulfanyl]acetate + [(propan-2-yl)sulfanyl]acetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dibutanoate + H2O
fluorescein-3'-oxymethyl butanoate + butanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dihexanoate + H2O
fluorescein-3'-oxymethyl hexanoate + hexanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene dipentanoate + H2O
fluorescein-3'-oxymethyl pentanoate + pentanoate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
S-formylglutathione + H2O
?
S-formylglutathione + H2O
glutathione + formate
S-lactoylglutathione + H2O
glutathione + lactate
additional information
?
-
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
(S)-D-lactoylglutathione + H2O
D-lactate + glutathione
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
artificial substrate of YeiG
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
artificial substrate of YeiG
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
Lota maculosa
-
very low activity
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
very low activity
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
very low activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
artificial substrate of FrmB and YeiG
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
artificial substrate of FrmB and YeiG
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
highest activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
artificial substrate of YeiG
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
hydrolysis of chiral substrates (4-chloro-3-hydroxybutyl acetate, 1-phenylethyl acetate, methyl mandelate) observed, esterification with n-propanol of chiral substrates (ketoprofen, ibuprofen) observed, esterification with butyl acid of chiral substrate (2-octanol) observed
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
artificial substrate of YeiG
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
artificial substrate of FrmB and YeiG
-
-
?
4-nitrophenyl thioacetate + H2O
4-nitrophenol + thioacetate
-
substrate with small acyl moiety
-
-
?
4-nitrophenyl thioacetate + H2O
4-nitrophenol + thioacetate
-
substrate with small acyl moiety
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O
[[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoic acid
i.e. POM-HEX, substrate is a prodrug of the compound HEX,which inhibits the glycolytic enzyme enolase
-
-
?
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O
[[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoic acid
i.e. POM-HEX, substrate is a prodrug of the compound HEX,which inhibits the glycolytic enzyme enolase
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O
fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O
fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O
fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate
-
-
-
?
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O
fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
Lota maculosa
-
very low activity
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
very low activity
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
very low activity
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
slight activity
-
ir
S-acetylglutathione + H2O
glutathione + acetate
Lota maculosa
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
substrate with small acyl moiety, high activity
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
substrate with small acyl moiety, high activity
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
-
1.3% of reaction rate with S-formylglutathione
-
?
S-formylglutathione + H2O
?
Kloeckera sp.
-
involved in the oxidation of methanol by methylotrophic yeasts
-
-
?
S-formylglutathione + H2O
?
-
part of the glutathione-dependent formaldehyde oxidation pathway
-
-
?
S-formylglutathione + H2O
?
-
detoxification of formaldehyde
-
-
?
S-formylglutathione + H2O
?
-
-
-
-
?
S-formylglutathione + H2O
?
-
dissimilatory pathway during growth on methanol
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
enzyme is involved in formaldehyde detoxification
-
?
S-formylglutathione + H2O
glutathione + formate
-
key enzyme catalyzes the final step of the formaldehyde detoxification, glutathione recycling
-
?
S-formylglutathione + H2O
glutathione + formate
-
key enzyme of the formaldehyde detoxification, glutathione recycling
-
?
S-formylglutathione + H2O
glutathione + formate
Dipodascus klebahnii
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
the substrate is an intermediate in the glutathione-dependent formaldehyde detoxification pathway
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
best substrate of FrmB and YeiG
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
the substrate is an intermediate in the glutathione-dependent formaldehyde detoxification pathway
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
ir
S-formylglutathione + H2O
glutathione + formate
Kloeckera sp.
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
Kloeckera sp.
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
Lota maculosa
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
substrate with small acyl moiety, lower activity than compared to S-acetylglutathione
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
substrate with small acyl moiety, lower activity than compared to S-acetylglutathione
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
Torulopsis pinus
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
-
enzyme is involved in the glutathione-dependent formaldehyde oxidation pathway during growth on methanol as the sole carbon source, regulation of gene expression
-
?
S-lactoylglutathione + H2O
glutathione + lactate
-
substrate of FrmB and YeiG
-
-
?
S-lactoylglutathione + H2O
glutathione + lactate
-
-
-
-
?
S-lactoylglutathione + H2O
glutathione + lactate
-
-
-
?
additional information
?
-
-
is unable to hydrolyse alpha-naphthyl dodecanoate, 4-nitrophenyl caprate, 4-nitrophenyl laurate, and 4-nitrophenyl palmitate. Potential role for Cys54 in regulation of enzyme activity through S-glutathionylation. Hydrolyzes C-O bonds with high affinity toward short to medium chain esters (C3-C4). Has more affinity toward C3 and C4 4-nitrophenyl esters than toward C3 and C4 alpha-naphthyl esters
-
-
?
additional information
?
-
-
2-nitrophenyl acetate is a poor substrate
-
?
additional information
?
-
-
the enzyme is a serine hydrolase rather than a cysteine hydrolase
-
-
?
additional information
?
-
-
no activity by FrmB and YeiG with S-(1,2-dicarboxyethyl)glutathione, S-hexylglutathione, and S-(4-nitrobenzyl)glutathione
-
-
?
additional information
?
-
-
no activity by FrmB and YeiG with S-(1,2-dicarboxyethyl)glutathione, S-hexylglutathione, and S-(4-nitrobenzyl)glutathione
-
-
?
additional information
?
-
-
esterase D/S-formylglutathione hydrolase plays a key role in glutathione-dependent detoxification of endogenously formed formaldehyde as well as in hydrolysis of various xenobiotics
-
-
?
additional information
?
-
-
PhEst contains a catalytic triad formed by residues Ser147, Asp225 and His258. It shows no activity toward substrates with bulky acyl groups such as S-lactoylglutathione. Has a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold
-
-
?
additional information
?
-
-
PhEst contains a catalytic triad formed by residues Ser147, Asp225 and His258. It shows no activity toward substrates with bulky acyl groups such as S-lactoylglutathione. Has a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold
-
-
?
additional information
?
-
enzyme shows modest activity with substrates 4-nitrophenyl acetate, 4-nitrophenyl butanoate, but not with 4-nitrophenyl trimethylacetate
-
-
-
additional information
?
-
enzyme shows modest activity with substrates 4-nitrophenyl acetate, 4-nitrophenyl butanoate, but not with 4-nitrophenyl trimethylacetate
-
-
-
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0.08
4-methyl-2-oxo-2H-chromen-7-yl (2E)-but-2-enoate
-
0.09
4-methyl-2-oxo-2H-chromen-7-yl 3,3-dimethylbutanoate
-
0.05
4-methyl-2-oxo-2H-chromen-7-yl 3-cyclopentylpropanoate
-
0.06
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbut-2-enoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbutanoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl 3-phenoxybutanoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl acetate
-
0.07
4-methyl-2-oxo-2H-chromen-7-yl butyrate
-
0.04
4-methyl-2-oxo-2H-chromen-7-yl cyclopentanecarboxylate
-
0.04
4-methyl-2-oxo-2H-chromen-7-yl heptanoate
-
0.09
4-methyl-2-oxo-2H-chromen-7-yl hexanoate
-
0.05
4-methyl-2-oxo-2H-chromen-7-yl pentanoate
-
0.1
4-methyl-2-oxo-2H-chromen-7-yl pivalate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl propionate
-
0.019
4-methylumbelliferyl acetate
-
-
0.013 - 3.5
4-nitrophenyl acetate
0.012 - 0.7
4-nitrophenyl butyrate
0.02 - 0.95
4-nitrophenyl caproate
0.05 - 0.83
4-nitrophenyl propionate
0.087 - 0.12
4-yethylumbelliferyl acetate
0.54 - 1.3
Alpha-naphthyl acetate
0.35
alpha-naphthyl propionate
-
in Tris-HCl buffer, pH 8.0
0.54
beta-naphthyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.03
fluorescein diacetate
-
recombinant enzyme, pH 7.2, 37°C
0.44
naphthalen-1-yl n-butanoate
-
in Tris-HCl buffer, pH 8.0
0.12 - 0.15
S-acetylglutathione
0.077 - 0.43
S-formylglutathione
0.58 - 3
S-Lactoylglutathione
0.013
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.054
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.054
4-nitrophenyl acetate
-
mutant W197I, pH 7.4, 22°C
0.1
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.14
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.14
4-nitrophenyl acetate
-
mutant W197I/C60S, pH 7.4, 22°C
0.15
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.16
4-nitrophenyl acetate
-
mutant H160S, pH 7.4, 22°C
0.18
4-nitrophenyl acetate
-
mutant Y278F, pH 7.4, 22°C
0.19
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.19
4-nitrophenyl acetate
-
mutant C60A, pH 7.4, 22°C
0.19
4-nitrophenyl acetate
-
mutant C60S, pH 7.4, 22°C
0.23
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.29
4-nitrophenyl acetate
-
pH 8.0, 37°C, recombinant FrmB
0.34
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.4
4-nitrophenyl acetate
-
wild-type, pH 7.4, 22°C
0.4
4-nitrophenyl acetate
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.45
4-nitrophenyl acetate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.48
4-nitrophenyl acetate
-
in Tris-HCl buffer, pH 8.0
0.49
4-nitrophenyl acetate
-
-
0.78
4-nitrophenyl acetate
-
mutant N64A, pH 7.4, 22°C
0.9
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.99
4-nitrophenyl acetate
-
mutant W197I/H160I, pH 7.4, 22°C
1.02
4-nitrophenyl acetate
-
recombinant enzyme, pH 7.2, 37°C
2.5
4-nitrophenyl acetate
-
mutant H160I, pH 7.4, 22°C
2.6
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
2.6
4-nitrophenyl acetate
-
mutant H160I oxidized form with catalase, pH 7.4, 22°C
3.5
4-nitrophenyl acetate
-
mutant H160I oxidized form, pH 7.4, 22°C
0.012
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.018
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.019
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.03
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.04
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.09
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.11
4-nitrophenyl butyrate
-
in Tris-HCl buffer, pH 8.0
0.12
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.13
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.14
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.19
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.2
4-nitrophenyl butyrate
Km less than 0.2 mM, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.7
4-nitrophenyl butyrate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.02
4-nitrophenyl caproate
-
in Tris-HCl buffer, pH 8.0
0.95
4-nitrophenyl caproate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.05
4-nitrophenyl propionate
-
in Tris-HCl buffer, pH 8.0
0.48
4-nitrophenyl propionate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.83
4-nitrophenyl propionate
-
pH 8.0, 37°C, recombinant FrmB
0.087
4-yethylumbelliferyl acetate
-
pH 7.0, 25°C
0.12
4-yethylumbelliferyl acetate
-
recombinant enzyme, pH 7.5, 37°C
0.54
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D255A
0.57
Alpha-naphthyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.8
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D80A
1.01
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D199A
1.03
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant wild-type YeiG
1.06
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant C26A
1.28
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant C54A
1.3
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D218A
0.12
S-acetylglutathione
-
-
0.15
S-acetylglutathione
-
recombinant enzyme, pH 7.2, 37°C
0.077
S-formylglutathione
Kloeckera sp.
-
-
0.13
S-formylglutathione
-
recombinant enzyme, pH 7.2, 37°C
0.2
S-formylglutathione
-
-
0.21
S-formylglutathione
-
-
0.29
S-formylglutathione
-
-
0.318
S-formylglutathione
-
pH 7.0, 25°C
0.41
S-formylglutathione
-
pH 8.0, 37°C, recombinant FrmB
0.43
S-formylglutathione
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.58
S-Lactoylglutathione
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.6
S-Lactoylglutathione
-
pH 8.0, 37°C, recombinant FrmB
0.9
S-Lactoylglutathione
-
mutant W197I/H160I, pH 7.4, 22°C
1.25
S-Lactoylglutathione
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3
S-Lactoylglutathione
-
wild-type, pH 7.4, 22°C
3
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3
S-Lactoylglutathione
-
mutant W197I/C60S, pH 7.4, 22°C
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0.0055 - 3.1
4-nitrophenyl acetate
0.003 - 4.48
4-nitrophenyl butyrate
0.49 - 0.67
4-nitrophenyl caproate
0.14 - 1.84
4-nitrophenyl propionate
2.17 - 5.12
Alpha-naphthyl acetate
1.9
alpha-naphthyl propionate
-
in Tris-HCl buffer, pH 8.0
1.73
naphthalen-1-yl n-butanoate
-
in Tris-HCl buffer, pH 8.0
6.51 - 28.5
S-formylglutathione
0.05 - 116.7
S-Lactoylglutathione
0.0055
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.028
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.048
4-nitrophenyl acetate
-
mutant W197I/H160I, pH 7.4, 22°C
0.1
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.26
4-nitrophenyl acetate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.3
4-nitrophenyl acetate
-
pH 8.0, 37°C, recombinant FrmB
0.32
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.48
4-nitrophenyl acetate
-
mutant H160S, pH 7.4, 22°C
0.525
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.6
4-nitrophenyl acetate
-
mutant Y278F, pH 7.4, 22°C
0.76
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.76
4-nitrophenyl acetate
-
mutant W197I/C60S, pH 7.4, 22°C
0.85
4-nitrophenyl acetate
-
mutant H160I, pH 7.4, 22°C
0.97
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.98
4-nitrophenyl acetate
-
mutant C60A, pH 7.4, 22°C
1.05
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.05
4-nitrophenyl acetate
-
mutant W197I, pH 7.4, 22°C
1.1
4-nitrophenyl acetate
-
mutant N64A, pH 7.4, 22°C
1.5
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.5
4-nitrophenyl acetate
-
mutant C60S, pH 7.4, 22°C
1.53
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.8
4-nitrophenyl acetate
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.8
4-nitrophenyl acetate
-
wild-type, pH 7.4, 22°C
1.95
4-nitrophenyl acetate
-
in Tris-HCl buffer, pH 8.0
2.8
4-nitrophenyl acetate
-
mutant H160I oxidized form with catalase, pH 7.4, 22°C
3.1
4-nitrophenyl acetate
-
mutant H160I oxidized form, pH 7.4, 22°C
0.003
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.0165
4-nitrophenyl butyrate
kcat less than 0.0165 s-1, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.04
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.078
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.2
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.36
4-nitrophenyl butyrate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.43
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.23
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.65
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.92
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.97
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3.63
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
4.48
4-nitrophenyl butyrate
-
in Tris-HCl buffer, pH 8.0
0.49
4-nitrophenyl caproate
-
pH 8.0, 37°C, recombinant wild-type YeiG
0.67
4-nitrophenyl caproate
-
in Tris-HCl buffer, pH 8.0
0.14
4-nitrophenyl propionate
-
pH 8.0, 37°C, recombinant FrmB
0.37
4-nitrophenyl propionate
-
pH 8.0, 37°C, recombinant wild-type YeiG
1.84
4-nitrophenyl propionate
-
in Tris-HCl buffer, pH 8.0
2.17
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D80A
2.23
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D255A
2.96
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D199A
3.13
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D218A
3.3
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant wild-type YeiG
3.81
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant D218A
5.09
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant wild-type YeiG
5.1
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant C54A
5.12
Alpha-naphthyl acetate
-
pH 8.0, 37°C, recombinant YeiG mutant C26A
6.51
S-formylglutathione
-
pH 8.0, 37°C, recombinant wild-type YeiG
28.5
S-formylglutathione
-
pH 8.0, 37°C, recombinant FrmB
0.05
S-Lactoylglutathione
-
pH 8.0, 37°C, recombinant FrmB
0.118
S-Lactoylglutathione
-
mutant W197I/H160I, pH 7.4, 22°C
1.02
S-Lactoylglutathione
-
pH 8.0, 37°C, recombinant wild-type YeiG
50
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
50
S-Lactoylglutathione
-
mutant W197I/C60S, pH 7.4, 22°C
116
S-Lactoylglutathione
-
wild-type, pH 7.4, 22°C
116.7
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
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C54S
-
shows a 4fold decrease in alpha-naphthyl butyrate activity. Is insensitive to the inhibitor N-ethylmaleimide
S147A
-
is unable to hydrolyse alpha-naphthyl butyrate
S152A
-
site-directed mutagenesis, completely inactive mutant
C26A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
C54A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
D199A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
D218A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
D223A
-
site-directed mutagenesis, the YeiG mutant shows no esterase activity
D255A
-
site-directed mutagenesis, the YeiG mutant shows 2fold reduced activity compared to the wild-type enzyme
D80A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
S154A
-
site-directed mutagenesis, the YeiG mutant shows no esterase activity
C26A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
-
C54A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
-
D199A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
-
D218A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
-
C60A
-
Km and kcat(4-nitrophenyl acetate) slightly decreased compared to wild-type
C60H/W197I
mutant shows significantly decreased activity
C60K/W197I
the mutation results in a further enhancement of the rates of phosphorylation with paraoxon but does not affect the dephosphorylation of the enzyme
C60Q/W197I
mutant shows significantly decreased activity
C60R/W197I
the mutation results in a further enhancement of the rates of phosphorylation with paraoxon but does not affect the dephosphorylation of the enzyme
C60S/W197I
mutant shows significantly decreased activity
G57H
mutant shows significantly decreased activity
H160I
-
Oxidation leads to activation of mutant enzyme. Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Oxidized form (with or without catalase): Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) increased compared to wild-type
H160S
-
Km (4-nitrophenyl acetate) slightly decreased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
L58H/W197I
mutant shows significantly decreased activity
M162H
mutant shows significantly decreased activity
M162H/C60S/W197I
mutant shows significantly decreased activity
N64A
-
Km (4-nitrophenyl acetate) slightly increased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
W197I/C60S
-
Km (4-nitrophenyl acetate) decreased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Km (S-lactolylglutathione) increased and kcat (4-nitrophenyl acetate) highly decreased compared to wild-type
W197I/H160I
-
Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Km (S-lactolylglutathione) decreased and kcat (4-nitrophenyl acetate) highly decreased compared to wild-type
Y278F
-
Km (4-nitrophenyl acetate) slightly decreased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
C59S
-
site-directed mutagenesis, the mutant shows no hydrolase activity with S-formylglutathione, but with 4-methylumbelliferyl acetate in contrast to the wild-type enzyme
C59S
-
mutant enzyme is highly active in hydrolysis of 4 -methylumbelliferyl acetate
C60S
mutant shows significantly decreased activity
C60S
-
Km and kcat(4-nitrophenyl acetate) slightly decreased compared to wild-type. mutant is not inactivated by peroxide
W197I
the substitution enhances SFGH reactivity with paraoxon by more than 1000fold thereby overcoming natural organophosphate resistance, the mutant increases the rate of organophosphate inhibition under pseudo-first-order conditions but does not accelerate organophosphate hydrolysis
W197I
-
Km (4-nitrophenyl acetate) decreased and kcat (4-nitrophenyl acetate) decreased compared to wild-type
additional information
-
construction of FrmB and YeiG deletion mutants
additional information
-
construction of FrmB and YeiG deletion mutants
-
additional information
-
fgh1 gene disruption impairs the ability to grow on methanol and reduces the growth rate on methylamine and choline as sole nitrogen source, while growth on glucose or glycerol is not affected
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Uotila, L.
Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases
Biochemistry
12
3938-3943
1973
Homo sapiens
brenda
Uotila, L.; Koivusalo, M.
Purification and properties of S-formylglutathione hydrolase from human liver
J. Biol. Chem.
249
7664-7672
1974
Homo sapiens
brenda
Uotila, L.; Koivusalo, M.
Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism
Arch. Biochem. Biophys.
196
33-45
1979
Pisum sativum
brenda
Uotila, L.
Glutathione thiol esterases of human red blood cells. Fractionation by gel electrophoresis and isoelectric focusing
Biochim. Biophys. Acta
580
277-288
1979
Homo sapiens
brenda
Kato, N.; Sakazawa, C.; Nishizawa, T.; Tani, Y.; Yamada, H.
Purificaton and characterization of S-formylglutathione hydrolase from a methanol-utilizing yeast, Kloeckera sp. No. 2201
Biochim. Biophys. Acta
611
323-332
1980
Kloeckera sp., Ogataea angusta, Ogataea trehalophila, Torulopsis pinus, [Candida] boidinii
brenda
Neben, I.; Sahm, H.; Kula, M.R.
Studies on an enzyme, S-formylglutathione hydrolase, of the dissimilatory pathway of methanol in Candida boidinii
Biochim. Biophys. Acta
614
81-91
1980
[Candida] boidinii
brenda
Uotila, L.; Koivusalo, M.
S-Formylglutathione hydrolase
Methods Enzymol.
77
320-325
1981
Escherichia coli, Homo sapiens
brenda
Kato, N.; Miyawaki, N.; Sakazawa, C.
Oxidation of formaldehyde by the resistant yeasts Debaryomyces vanriji and Trichosporon penicillatum
Agric. Biol. Chem.
46
655-661
1982
Schwanniomyces vanrijiae, Kloeckera sp., Dipodascus klebahnii
-
brenda
Allais, J.J.; Louktibi, A.; Baratti, J.
Oxidation of methanol by the yeast, Pichia pastoris. Purification and properties of the formaldehyde dehydrogenase
Agric. Biol. Chem.
47
1509-1516
1983
Komagataella pastoris, Komagataella pastoris IFP 206
-
brenda
Degrassi, G.; Uotila, L.; Klima, R.; Venturi, V.
Purification and properties of an esterase from the yeast Saccharomyces cerevisiae and identification of the encoding gene
Appl. Environ. Microbiol.
65
3470-3472
1999
Saccharomyces cerevisiae
brenda
Harms, N.; Ras, J.; Reijnders, M.; van Spanning, R.J.M.; Stouthamer, A.H.
S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?
J. Bacteriol.
178
6296-6299
1996
Paracoccus denitrificans
brenda
Uotila, L.; Koivusalo, M.
Expression of formaldehyde dehydrogenase and S-formylglutathione hydrolase activities in different rat tissues
Adv. Exp. Med. Biol.
414
365-371
1997
Rattus norvegicus
brenda
Koivusalo, M.; Lapatto, R.; Uotila, L.
Purification and characterization of S-formylglutathione hydrolase from human, rat and fish tissues
Adv. Exp. Med. Biol.
372
427-434
1995
Homo sapiens, Lota maculosa, Rattus norvegicus
brenda
McAuley, K.E.; Cummins, I.; Papiz, M.; Edwards, R.; Fordham-Skelton, A.P.
Purification, crystallization and preliminary X-ray diffraction analysis of S-formylglutathione hydrolase from Arabidopsis thaliana: effects of pressure and selenomethionine substitution on space-group changes
Acta Crystallogr. Sect. D
59
2272-2274
2003
Arabidopsis thaliana
brenda
Kordic, S.; Cummins, I.; Edwards, R.
Cloning and characterization of an S-formylglutathione hydrolase from Arabidopsis thaliana
Arch. Biochem. Biophys.
399
232-238
2002
Arabidopsis thaliana
brenda
Yurimoto, H.; Lee, B.; Yano, T.; Sakai, Y.; Kato, N.
Physiological role of S-formylglutathione hydrolase in C(1) metabolism of the methylotrophic yeast Candida boidinii
Microbiology
149
1971-1979
2003
[Candida] boidinii
brenda
Haslam, R.; Rust, S.; Pallett, K.; Cole, D.; Coleman, J.
Cloning and characterisation of S-formylglutathione hydrolase from Arabidopsis thaliana: a pathway for formaldehyde detoxification
Plant Physiol. Biochem.
40
281-288
2002
Arabidopsis thaliana
-
brenda
Gonzalez, C.F.; Proudfoot, M.; Brown, G.; Korniyenko, Y.; Mori, H.; Savchenko, A.V.; Yakunin, A.F.
Molecular basis of formaldehyde detoxification: Characterization of two s-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG
J. Biol. Chem.
282
14514-14522
2006
Escherichia coli, Escherichia coli BW25113
brenda
Cummins, I.; McAuley, K.; Fordham-Skelton, A.; Schwoerer, R.; Steel, P.G.; Davis, B.G.; Edwards, R.
Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase
J. Mol. Biol.
359
422-432
2006
Arabidopsis thaliana
brenda
Stover, N.A.; Cavalcanti, A.R.O.; Li, A.J.; Richardson, B.C.; Landweber, L.F.
Reciprocal fusions of two genes in the formaldehyde detoxification pathway in ciliates and diatoms [Erratum to document cited in CA143:433476]
Mol. Biol. Evol.
22
1749
2005
Phaeodactylum tricornutum, Tetrahymena thermophila, Thalassiosira pseudonana, Sterkiella histriomuscorum (Q4QXY1)
-
brenda
Cummins, I.; Landrum, M.; Steel, P.G.; Edwards, R.
Structure activity studies with xenobiotic substrates using carboxylesterases isolated from Arabidopsis thaliana
Phytochemistry
68
811-818
2007
Arabidopsis thaliana (Q8LAS8), Arabidopsis thaliana
brenda
Cummins, I.; Steel, P.G.; Edwards, R.
Identification of a carboxylesterase expressed in protoplasts using fluorescence-activated cell sorting
Plant Biotechnol. J.
5
354-359
2007
Arabidopsis thaliana
brenda
Legler, P.M.; Kumaran, D.; Swaminathan, S.; Studier, F.W.; Millard, C.B.
Structural characterization and reversal of the natural organophosphate resistance of a D-type esterase, Saccharomyces cerevisiae S-formylglutathione hydrolase
Biochemistry
47
9592-9601
2008
Saccharomyces cerevisiae (P40363), Saccharomyces cerevisiae
brenda
Tuin, A.W.; Mol, M.A.; van den Berg, R.M.; Fidder, A.; van der Marel, G.A.; Overkleeft, H.S.; Noort, D.
Activity-based protein profiling reveals broad reactivity of the nerve agent sarin
Chem. Res. Toxicol.
22
683-689
2009
Homo sapiens
brenda
Kaschani, F.; Gu, C.; Niessen, S.; Hoover, H.; Cravatt, B.F.; Van der Hoorn, R.A.
Diversity of serine hydrolase activities of unchallenged and Botrytis-infected Arabidopsis thaliana
Mol. Cell. Proteomics
8
1082-1093
2009
Arabidopsis thaliana
brenda
Alterio, V.; Aurilia, V.; Romanelli, A.; Parracino, A.; Saviano, M.; D'Auria, S.; De Simone, G.
Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125
Biopolymers
93
669-677
2010
Pseudoalteromonas haloplanktis, Pseudoalteromonas haloplanktis TAC 125
brenda
van Straaten, K.E.; Gonzalez, C.F.; Valladares, R.B.; Xu, X.; Savchenko, A.V.; Sanders, D.A.
The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens
Protein Sci.
18
2196-2202
2009
Agrobacterium tumefaciens
brenda
Parracino, A.; Gajula, G.; di Gennaro, A.; Neves-Petersen, M.; Rafaelsen, J.; Petersen, S.
Towards nanoscale biomedical devices in medicine: Biofunctional and spectroscopic characterization of superparamagnetic nanoparticles
J. Fluoresc.
21
663-672
2011
Pseudoalteromonas haloplanktis, Pseudoalteromonas haloplanktis TAC 125
brenda
Liu, J.; Tang, X.; Wang, B.; Yu, H.; Min, H.
Cloning, screening and characterization of ester hydrolases with enantioselectivity in typical bacteria
Process Biochem.
45
475-480
2010
Pseudomonas putida (Q88MF4)
-
brenda
Legler, P.M.; Leary, D.H.; Hervey, W.J.; Millard, C.B.
A role for His-160 in peroxide inhibition of S. cerevisiae S-formylglutathione hydrolase: evidence for an oxidation sensitive motif
Arch. Biochem. Biophys.
528
7-20
2012
Saccharomyces cerevisiae
brenda
Li, W.; Zhu, Z.; Cao, W.; Yang, F.; Zhang, X.; Li, D.; Zhang, K.; Li, P.; Mao, R.; Liu, X.; Zheng, H.
Esterase D enhances type I interferon signal transduction to suppress foot-and-mouth disease virus replication
Mol. Immunol.
75
112-121
2016
Sus scrofa (Q9GJT2)
brenda
Xu, Y.; Sun, Z.
Regulation of S-formylglutathione hydrolase by the anti-aging gene klotho
Oncotarget
8
88259-88275
2017
Homo sapiens, Mus musculus
brenda
Huetten, M.; Geukes, M.; Misas-Villamil, J.C.; van der Hoorn, R.A.; Grundler, F.M.; Siddique, S.
Activity profiling reveals changes in the diversity and activity of proteins in Arabidopsis roots in response to nematode infection
Plant Physiol. Biochem.
97
36-43
2015
Arabidopsis thaliana (Q8LAS8)
brenda
Miller, J.J.; Shah, I.T.; Hatten, J.; Barekatain, Y.; Mueller, E.A.; Moustafa, A.M.; Edwards, R.L.; Dowd, C.S.; Planet, P.; Muller, F.L.; Jez, J.; Odom John, A.R.
Structure-guided microbial targeting of antistaphylococcal prodrugs
eLife
10
e66657
2021
Staphylococcus aureus (Q2FUY3), Staphylococcus aureus PS 47 (Q2FUY3)
brenda