BRENDA - Enzyme Database
show all sequences of 3.1.2.12

Structural characterization and reversal of the natural organophosphate resistance of a D-type esterase, Saccharomyces cerevisiae S-formylglutathione hydrolase

Legler, P.M.; Kumaran, D.; Swaminathan, S.; Studier, F.W.; Millard, C.B.; Biochemistry 47, 9592-9601 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary)
Crystallization (Commentary)
Organism
sitting drop vapour diffusion method, using 0.17 M ammonium acetate, 0.085 M sodium acetate trihydrate (pH 4.6), 25.5% (w/v) PEG 4000, and 15% (v/v) glycerol
Saccharomyces cerevisiae
Engineering
Protein Variants
Commentary
Organism
C60H/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
C60Q/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
C60S
mutant shows significantly decreased activity
Saccharomyces cerevisiae
C60S/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
G57H
mutant shows significantly decreased activity
Saccharomyces cerevisiae
L58H/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
M162H
mutant shows significantly decreased activity
Saccharomyces cerevisiae
M162H/C60S/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
Hg2+
susceptible to inhibition by Hg2+
Saccharomyces cerevisiae
methyl paraoxon
-
Saccharomyces cerevisiae
paraoxon
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.013
-
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.018
-
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.019
-
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.03
-
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.04
-
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.054
-
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.09
-
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.1
-
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.12
-
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.13
-
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.14
-
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.14
-
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.15
-
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.19
-
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.19
-
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.23
-
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.34
-
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.9
-
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.25
-
S-Lactoylglutathione
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
2.6
-
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
3
-
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C; mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33930
-
calculated from amino acid sequence
Saccharomyces cerevisiae
33934
-
1 * 33934, calculated from amino acid sequence
Saccharomyces cerevisiae
67800
-
gel filtration
Saccharomyces cerevisiae
Organism
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
P40363
-
-
Oxidation Stability
Oxidation Stability
Organism
the wild type enzyme is sensitive to oxidation
Saccharomyces cerevisiae
Purification (Commentary)
Purification (Commentary)
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4-nitrophenyl acetate + H2O
-
691005
Saccharomyces cerevisiae
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
691005
Saccharomyces cerevisiae
4-nitrophenol + butyrate
-
-
-
?
paraoxon + H2O
-
691005
Saccharomyces cerevisiae
diethylphosphate + 4-nitrophenol
-
-
-
?
S-formylglutathione + H2O
-
691005
Saccharomyces cerevisiae
glutathione + formate
-
-
-
?
S-lactoylglutathione + H2O
-
691005
Saccharomyces cerevisiae
glutathione + lactate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
the wild type enzyme crystallizes as a dimer of dimers with four molecules in the asymmetric unit, X-ray crystallography
Saccharomyces cerevisiae
monomer
1 * 33934, calculated from amino acid sequence
Saccharomyces cerevisiae
Synonyms
Synonyms
Commentary
Organism
esterase D
-
Saccharomyces cerevisiae
SFGH
-
Saccharomyces cerevisiae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.003
-
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.0055
-
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.028
-
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.04
-
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.078
-
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.1
-
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.2
-
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.32
-
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.43
-
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.525
-
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.76
-
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.97
-
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.05
-
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.23
-
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.5
-
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.53
-
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.65
-
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
1.92
-
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.97
-
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
3.63
-
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
50
-
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
116.7
-
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting drop vapour diffusion method, using 0.17 M ammonium acetate, 0.085 M sodium acetate trihydrate (pH 4.6), 25.5% (w/v) PEG 4000, and 15% (v/v) glycerol
Saccharomyces cerevisiae
Engineering (protein specific)
Protein Variants
Commentary
Organism
C60H/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
C60Q/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
C60S
mutant shows significantly decreased activity
Saccharomyces cerevisiae
C60S/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
G57H
mutant shows significantly decreased activity
Saccharomyces cerevisiae
L58H/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
M162H
mutant shows significantly decreased activity
Saccharomyces cerevisiae
M162H/C60S/W197I
mutant shows significantly decreased activity
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Hg2+
susceptible to inhibition by Hg2+
Saccharomyces cerevisiae
methyl paraoxon
-
Saccharomyces cerevisiae
paraoxon
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.013
-
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.018
-
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.019
-
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.03
-
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.04
-
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.054
-
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.09
-
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.1
-
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.12
-
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.13
-
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.14
-
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.14
-
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.15
-
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.19
-
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.19
-
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.23
-
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.34
-
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.9
-
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.25
-
S-Lactoylglutathione
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
2.6
-
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
3
-
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C; mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33930
-
calculated from amino acid sequence
Saccharomyces cerevisiae
33934
-
1 * 33934, calculated from amino acid sequence
Saccharomyces cerevisiae
67800
-
gel filtration
Saccharomyces cerevisiae
Oxidation Stability (protein specific)
Oxidation Stability
Organism
the wild type enzyme is sensitive to oxidation
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4-nitrophenyl acetate + H2O
-
691005
Saccharomyces cerevisiae
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
691005
Saccharomyces cerevisiae
4-nitrophenol + butyrate
-
-
-
?
paraoxon + H2O
-
691005
Saccharomyces cerevisiae
diethylphosphate + 4-nitrophenol
-
-
-
?
S-formylglutathione + H2O
-
691005
Saccharomyces cerevisiae
glutathione + formate
-
-
-
?
S-lactoylglutathione + H2O
-
691005
Saccharomyces cerevisiae
glutathione + lactate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
the wild type enzyme crystallizes as a dimer of dimers with four molecules in the asymmetric unit, X-ray crystallography
Saccharomyces cerevisiae
monomer
1 * 33934, calculated from amino acid sequence
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.003
-
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.0055
-
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
0.028
-
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.04
-
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.078
-
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.1
-
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.2
-
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.32
-
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.43
-
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.525
-
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.76
-
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
0.97
-
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.05
-
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.23
-
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.5
-
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.53
-
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.65
-
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
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 22C
Saccharomyces cerevisiae
1.92
-
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
1.97
-
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
3.63
-
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
50
-
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
116.7
-
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22C
Saccharomyces cerevisiae
Other publictions for EC 3.1.2.12
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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682300
Cummins
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Kato
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Neben
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80983
Uotila
Purification of formaldehyde a ...
Pisum sativum
Arch. Biochem. Biophys.
196
33-45
1979
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80984
Uotila
Glutathione thiol esterases of ...
Homo sapiens
Biochim. Biophys. Acta
580
277-288
1979
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80982
Uotila
Purification and properties of ...
Homo sapiens
J. Biol. Chem.
249
7664-7672
1974
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14
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14
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80981
Uotila
Preparation and assay of gluta ...
Homo sapiens
Biochemistry
12
3938-3943
1973
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