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EC Tree
IUBMB Comments Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa The enzyme appears in selected viruses and cellular organisms
Synonyms
esterase, carboxylesterase, butyrate esterase, carboxyl esterase, carboxylesterase 1, egasyn, serine protease-like, hce-2, acyl coenzyme a:cholesterol acyltransferase, esterase a,
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Acyl coenzyme A:cholesterol acyltransferase
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alpha-carboxylesterase
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Brain carboxylesterase hBr1
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butyrate esterase
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Carboxyesterase ES-10
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carboxyl ester hydrolase
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carboxylate esterase
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Carboxylesterase-5C
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carboxylic acid esterase
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carboxylic ester hydrolase
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carboxylic esterase
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Carboxylic-ester hydrolase
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esterase, carboxyl
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Kidney microsomal carboxylesterase
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Liver microsomal carboxylesterase
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methylbutyrate esterase
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Microsomal palmitoyl-CoA hydrolase
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Monocyte/macrophage serine esterase
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Non-specific carboxylesterase
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nonspecific carboxylesterase
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procaine esterase
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Proline-beta-naphthylamidase
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propionyl esterase
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triacetin esterase
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vitamin A esterase
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PA3859
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hydrolysis of carboxylic ester
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carboxylic-ester hydrolase
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
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p-nitrophenyl palmitate
p-nitrophenol + palmitate
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?
1-naphthyl acetate + H2O
1-naphthol + acetate
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1-naphthyl butanoate + H2O
1-naphthol + butanoate
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54% of the activity with 1-naphthyl acetate
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1-naphthyl caprylate + H2O
1-naphthol + caprylate
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14% of the activity with 1-naphthyl acetate
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?
1-naphthyl laurate + H2O
1-naphthol + laurate
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9% of the activity with 1-naphthyl acetate
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?
1-naphthyl oleate + H2O
1-naphthol + oleate
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2% of the activity with 1-naphthyl acetate
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4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
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?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
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?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
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4-nitrophenyl heptanoate + H2O
4-nitrophenol + heptanoate
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4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
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4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
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4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
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4-nitrophenyl nonanoate + H2O
4-nitrophenol + nonanoate
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4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
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4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
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4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
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4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
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4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
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carboxyfluorescein diacetate + H2O
carboxyfluorescein + acetate
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fluorescein diacetate + H2O
fluorescein + acetate
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?
additional information
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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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additional information
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PA3859 displays similar affinity for 4-nitrophenyl substrates with acyl chains from C8 to C18
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additional information
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PA3859 displays similar affinity for 4-nitrophenyl substrates with acyl chains from C8 to C18
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MgCl2
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slight activation
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CoCl2
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1mM, 34% residual activity
CuCl2
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1 mM, 59% residual activity
dithiothreitol
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1 mM, 58% residual activity
FeCl2
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1 mM, 40% residual activity
FeCl3
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1 mM, 38% residual activity
NiCl2
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1 mM, 35% residual activity
phenylmethylsulfonyl fluoride
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0.1 mM, 48% residual activity
ZnCl2
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1 mM, 36% residual activity
additional information
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not inhibitory: EDTA
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0.43
4-nitrophenyl acetate
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pH 9.0, 25°C
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3000
1-naphthyl acetate
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1600
1-naphthyl butanoate
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6400
4-nitrophenyl acetate
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1700
4-nitrophenyl butanoate
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8500
4-yethylumbelliferyl acetate
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2800
carboxyfluorescein diacetate
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170
fluorescein diacetate
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5.2
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isoelectric focusing
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SwissProt
brenda
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enzyme is located in the outer membrane with the catalytic domain exposed to the surface
brenda
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autotransporter protein which exposes its catalytically active esterase domain on the cell surface
brenda
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66000
x * 66000, SDS-PAGE
24691
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1 * 28000, SDS-PAGE, 1 * 24691, ESI-MS
28000
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1 * 28000, SDS-PAGE, 1 * 24691, ESI-MS
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monomer
1 * 24000, SDS-PAGE
monomer
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1 * 28000, SDS-PAGE, 1 * 24691, ESI-MS
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hanging drop vapor diffusion method, using PEGMME 5000 as precipitant
two crystal forms, form I in space group P21, resoöution 2.9A, form II, space group P21212, 2.1 A resolution
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S38A
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catalytically inactive mutant, strains show defects in rhamnolipid production, swarming, swimming and twitching motility and biofilm formation
additional information
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overexpression of isoform EstA in wild-type background results in an increased production of rhamnolipids, whereas an enzyme deletion mutant produces only marginal amounts of rhamnolipids. In the deletion mutant, cellular motility and biofilm formation are also affected
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50
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pH 9.0, 2 h, stable up to 50°C
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expression in Escherichia coli
expressed in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli, N-terminal His-tag
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Pesaresi, A.; Devescovi, G.; Lamba, D.; Venturi, V.; Degrassi, G.
Isolation, characterization, and heterologous expression of a carboxylesterase of Pseudomonas aeruginosa PAO1
Curr. Microbiol.
50
102-109
2005
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO1
brenda
Wilhelm, S.; Tommassen, J.; Jaeger, K.E.
A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
J. Bacteriol.
181
6977-6986
1999
Pseudomonas aeruginosa (O33407), Pseudomonas aeruginosa
brenda
Pesaresi, A.; Lambda, D.
Crystallization, X-ray diffraction analysis and phasing of carboxylesterase PA3859 from Pseudomonas aeruginosa
Biochim. Biophys. Acta
1752
197-201
2008
Pseudomonas aeruginosa
brenda
Wilhelm, S.; Gdynia, A.; Tielen, P.; Rosenau, F.; Jaeger, K.E.
The autotransporter esterase EstA of Pseudomonas aeruginosa is required for rhamnolipid production, cell motility, and biofilm formation
J. Bacteriol.
189
6695-6703
2007
Pseudomonas aeruginosa
brenda
Pesaresi, A.; Lamba, D.
Insights into the fatty acid chain length specificity of the carboxylesterase PA3859 from Pseudomonas aeruginosa: A combined structural, biochemical and computational study
Biochimie
92
1787-1792
2010
Pseudomonas aeruginosa (Q9HXE7), Pseudomonas aeruginosa
brenda
Transporter Classification Database (TCDB):
1.B.12.5.9