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Information on EC 3.1.1.6 - acetylesterase and Organism(s) Escherichia coli and UniProt Accession P23872

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.6 acetylesterase
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Escherichia coli
UNIPROT: P23872 not found.
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetyl esterase
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Acetic ester hydrolase
-
-
-
-
Acetyl esterase
acetyl-esterase
-
-
C-esterase
-
-
-
-
Chloroesterase
-
-
-
-
Citrus acetylesterase
-
-
-
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p-nitrophenyl acetate esterase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetic-ester acetylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9000-82-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-butanoate + H2O
4-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
activated Sepharose CL6B-bound activity, pH 8
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 0.19
4-nitrophenyl butyrate
0.015 - 0.073
tributyrin
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29 - 113
4-nitrophenyl butyrate
6.2 - 17.5
tributyrin
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.98
4-nitrophenyl acetate
at pH 7.0 and 39°C
0.057 - 0.26
4-nitrophenyl butyrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
250
-
pH 7.1, 65°C, purified recombinant wild-type enzyme
270
-
pH 7.1, 65°C, purified recombinant mutant T74A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 75
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
determined by affinity using pull down
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
His-tagged protein
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recombinant wild-type and mutant enzymes from strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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overexpression of wild-type and mutant enzymes in strain BL21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reversible unfolding of enzyme with both urea and guanidinium-HCl. Unfolding data suggest the presence of two domains which unfold more or less independently
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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protein-protein interaction consensus sequence, involved in regulation of both sugar and lipid metabolism, according to interaction partners
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team