We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
carbohydrate esterase, acetylesterase, est-4, haemagglutinin-esterase, pectin acetylesterase, est24, acetyl-esterase, tm0077, c20orf3, p-nitrophenyl acetate esterase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acetic ester hydrolase
-
-
-
-
Citrus acetylesterase
-
-
-
-
p-nitrophenyl acetate esterase
-
-
-
-
Acetyl esterase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of carboxylic ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetic-ester acetylhydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
tributyrin + H2O
?
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl-butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
additional information
?
-
-
activated Sepharose CL6B-bound activity, pH 8
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
106.21% activity at 0.5 mM
Co2+
105.61% activity at 0.5 mM
Ni2+
110.32% activity at 0.5 mM
Zn2+
103.63% activity at 0.5 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
77.86% residual activity at 2 mM
Fe3+
77.37% residual activity at 2 mM
K+
79.8% residual activity at 2 mM
Mg2+
67.81% residual activity at 2 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.13 - 0.19
4-nitrophenyl butyrate
0.84
4-nitrophenyl acetate
at pH 7.0 and 39°C
0.057 - 0.26
4-nitrophenyl butyrate
0.245 - 0.355
4-nitrophenyl hexanoate
0.75 - 2
4-nitrophenyl-butanoate
0.13
4-nitrophenyl butyrate
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.14
4-nitrophenyl butyrate
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.16
4-nitrophenyl butyrate
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.18
4-nitrophenyl butyrate
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.19
4-nitrophenyl butyrate
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.015
tributyrin
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.018
tributyrin
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.047
tributyrin
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.052
tributyrin
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.073
tributyrin
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.057
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.069
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.17
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.26
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.245
4-nitrophenyl hexanoate
-
pH 7.1, 65°C, recombinant wild-type enzyme
0.355
4-nitrophenyl hexanoate
-
pH 7.1, 65°C, recombinant mutant T74A
0.75
4-nitrophenyl-butanoate
-
pH 7.1, 25°C, recombinant wild-type enzyme
1.5
4-nitrophenyl-butanoate
-
pH 7.1, 65°C, recombinant wild-type enzyme
2
4-nitrophenyl-butanoate
-
pH 7.1, 65°C, recombinant mutant T74A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
29 - 113
4-nitrophenyl butyrate
0.82
4-nitrophenyl acetate
at pH 7.0 and 39°C
29 - 340
4-nitrophenyl butyrate
34.5 - 48.8
4-nitrophenyl hexanoate
21 - 155
4-nitrophenyl-butanoate
29
4-nitrophenyl butyrate
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
29
4-nitrophenyl butyrate
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
78
4-nitrophenyl butyrate
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
86
4-nitrophenyl butyrate
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
113
4-nitrophenyl butyrate
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
6.2
tributyrin
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
6.9
tributyrin
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
9.3
tributyrin
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
17.4
tributyrin
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
17.5
tributyrin
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
29
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
37
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
240
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
340
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
34.5
4-nitrophenyl hexanoate
-
pH 7.1, 65°C, recombinant wild-type enzyme
48.8
4-nitrophenyl hexanoate
-
pH 7.1, 65°C, recombinant mutant T74A
21
4-nitrophenyl-butanoate
-
pH 7.1, 25°C, recombinant wild-type enzyme
145
4-nitrophenyl-butanoate
-
pH 7.1, 65°C, recombinant wild-type enzyme
155
4-nitrophenyl-butanoate
-
pH 7.1, 65°C, recombinant mutant T74A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.98
4-nitrophenyl acetate
at pH 7.0 and 39°C
0.057 - 0.26
4-nitrophenyl butyrate
0.057
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.069
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.17
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.26
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
250
-
pH 7.1, 65°C, purified recombinant wild-type enzyme
270
-
pH 7.1, 65°C, purified recombinant mutant T74A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 9
about 35% activity at pH 7.0, 100% activity at pH 8.0, about 60% activity at pH 9.0, almost no activity below pH 6.0 and above pH 10.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40000
-
x * 40000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
determined by affinity using pull down
?
x * 38000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
His-tagged protein, both in the native form and with selenomethionine substitution
-
structural superimposition of homology-generated model with Alicyclobacillus acidocaldarius EST2 and Escherichia coli beta-cystathionase MalY revealed nine amino acid consensus sequence putatively involved in protein-protein interactions, amino acids 178-184 are putative core of interaction with MalY and MalT
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
R48A
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (3.7fold with 4-nitrophenyl butyrate and 8fold with tributyrin as substrate)
R48E
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (3.4fold with 4-nitrophenyl butyrate and 1.3fold with tributyrin as substrate)
R48K
the catalytic efficiency of the mutant is similar to the wild type enzyme
R48S
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (2.6fold with 4-nitrophenyl butyrate and 9.7fold with tributyrin as substrate)
L209F
-
the mutant shows 3.8fold increased activity compared to the wild type enzyme
L97F
-
the mutant shows 5.4fold increased activity compared to the wild type enzyme
L97F/L209F
-
the mutant shows 28.8fold increased activity compared to the wild type enzyme
R179A
-
mutation in interaction consensus sequence, wild-type activity, loss of interaction with Aes interactors such as MalY
T74A
-
random mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
V20D
-
site-directed mutagenesis, the mutant shows slightly reduced thermal stability compared to the wild-type enzyme, kinetic analysis, overview
additional information
-
random mutagenesis and screening for thermostable mutants at 85°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35 - 51
the enzyme maintains more than 80% activity between 35 and 51°C
55
-
the wild type enzyme shows a half-life of 40 min at 55°C
61
-
denaturation of Aes mutant V20D, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition
65
-
t1/2 inactivation is 5 min for the wild-type enzyme, and 30 min for mutant T74A, thermal inactivation first-order kinetics, overview
68
-
denaturation of Aes, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate precipitation and DEAE cellulose column chromatography
from bacterial extracts by binding to CNBr-activated Sepharose CL6B, 1.5 mg bound protein per ml resin, pH 8.3, 0.1 M sodium hydrogen carbonate, 0.5 M sodium chloride
-
recombinant wild-type and mutant enzymes from strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli JM109 cells
-
expressed in Escherichia coli JM110 cells
gene ybaC, overexpression of wild-type and mutant enzymes
-
overexpression of wild-type and mutant enzymes in strain BL21(DE3)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
reversible unfolding of enzyme with both urea and guanidinium-HCl. Unfolding data suggest the presence of two domains which unfold more or less independently
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
molecular biology
-
protein-protein interaction consensus sequence, involved in regulation of both sugar and lipid metabolism, according to interaction partners
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gerber, K.; Schiefner, A.; Seige, P.; Diederichs, K.; Boos, W.; Welte, W.
Crystallization and preliminary x-ray analysis of Aes, an acetyl-esterase from Escherichia coli
Acta Crystallogr. Sect. D
D60
531-533
2004
Escherichia coli
brenda
Del Vecchio, P.; Graziano, G.; Granata, V.; Farias, T.; Barone, G.; Mandrich, L.; Rossi, M.; Manco, G.
Denaturant-induced unfolding of the acetyl-esterase from Escherichia coli
Biochemistry
43
14637-14643
2004
Escherichia coli
brenda
Farias, T.; Mandrich, L.; Rossi, M.; Manco, G.
Biochemical and thermostability features of acetyl esterase Aes from Escherichia coli
Protein Pept. Lett.
14
165-169
2007
Escherichia coli
brenda
Del Vecchio, P.; Graziano, G.; Barone, G.; Mandrich, L.; Rossi, M.; Manco, G.
Temperature-induced denaturation of Aes acetyl-esterase from Escherichia coli
Thermochim. Acta
441
144-149
2006
Escherichia coli
-
brenda
DAmbrosio, C.; Mandrich, L.; Rossi, M.; Scaloni, A.; Manco, G.
A proteomic approach to study Escherichia coli. Acetyl esterase interactors unveil a sequence motif involved in protein-protein interaction
Protein Pept. Lett.
15
333-340
2008
Escherichia coli
brenda
Kobayashi, R.; Hirano, N.; Kanaya, S.; Saito, I.; Haruki, M.
Enhancement of the enzymatic activity of Escherichia coli acetyl esterase by random mutagenesis
J. Mol. Catal. B
67
155-161
2010
Escherichia coli (P23872)
-
brenda
Kobayashi, R.; Hirano, N.; Kanaya, S.; Haruki, M.
Enhancement of the enzymatic activity of Escherichia coli acetyl esterase by a double mutation obtained by random mutagenesis
Biosci. Biotechnol. Biochem.
76
2082-2088
2012
Escherichia coli
brenda
Wu, Z.; Chen, J.; Zhang, Z.; Ma, L.; Xu, T.; Yu, H.; Zhang, Q.; Chen, Y.
Development of Escherichia coli strain with enhanced enzymatic activity of acetyl esterase using a strategy of tandem repetitive promoters
Waste Biomass Valor.
8
2339-2348
2017
Escherichia coli (A0A0A7HLG5), Escherichia coli RB3 (A0A0A7HLG5)
-
brenda
Wu, Z.; Chen, J.; Zhang, Z.; Ma, L.; Xu, T.; Yu, H.; Zhang, Q.; Chen, Y.
Overexpression of Escherichia coli acetyl esterase using a strategy of multi-copy promoters
Waste Biomass Valor.
9
561-570
2018
Escherichia coli (A0A0A7HLG5), Escherichia coli RB3 (A0A0A7HLG5)
-
brenda