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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: Escherichia coli 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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additional information
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the enzyme belongs to the BioH enzyme family
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a carboxylic ester + H2O = an alcohol + a carboxylate
active site structure, catalytic triad consists of residues Ser82, His235, and Asp207
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hydrolysis of carboxylic or thio-esters
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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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4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
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4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
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p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
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p-nitrophenyl butyrate
p-nitrophenol + butyrate
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p-nitrophenyl caprate
p-nitrophenol + caprate
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p-nitrophenyl caproate
p-nitrophenol + caproate
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p-nitrophenyl laurate
p-nitrophenol + laurate
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p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
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p-nitrophenyl propionate
p-nitrophenol + propionate
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p-nitrophenyl stearate
p-nitrophenol + stearate
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palmitoyl-CoA
CoA + palmitate
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1-naphthyl acetate + H2O
1-naphthol + acetate
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1-naphthyl butyrate + H2O
1-naphthol + butyrate
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1-naphthyl propionate + H2O
1-naphthol + propionate
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2-naphthyl acetate + H2O
2-naphthol + acetate
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2-naphthyl butyrate + H2O
2-naphthol + butyrate
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2-naphthyl propionate + H2O
2-naphthol + propionate
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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
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4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
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4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
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p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
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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
best substrate
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
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additional information
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enzyme shows low thioesterase activity, it cannot use free pimelic acid for pimeloyl-CoA synthesis, enzyme shows a broad substrate specificity with a preference for short chain substrates
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additional information
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enzyme shows low thioesterase activity, it cannot use free pimelic acid for pimeloyl-CoA synthesis, enzyme shows a broad substrate specificity with a preference for short chain substrates
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additional information
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the enzyme BioH is involved in biotin biosynthesis
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additional information
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the enzyme BioH is involved in biotin biosynthesis
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additional information
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BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase
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additional information
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additional information
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the enzyme BioH is involved in biotin biosynthesis
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additional information
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the enzyme BioH is involved in biotin biosynthesis
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additional information
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BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase
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additional information
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no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHe is no metalloenzyme
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Phenylmethylsulfonylfluoride
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1-butanol
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62% inhibition of BioHe at 30%
acetone
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15% inhibition of BioHe at 30%
acetonitrile
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89% inhibition of BioHe at 30%
ethanol
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16% inhibition of BioHe at 30%
Fe2+
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1 mM, 10% loss of activity
Hg2+
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1 mM, 50% loss of activity
Isopropanol
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70% inhibition of BioHe at 30%
methanol
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7% inhibition of BioHe at 30%
SDS
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52% inhibition of recombinant BioHe at 0.2%
Zn2+
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1 mM, 75% loss of activity
additional information
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no inhibition by DMSO at 10-30%
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Cu2+
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1 mM, 14% loss of activity
Cu2+
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30% inhibition of recombinant BioHe at 5-10 mM
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Co2+
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150% activation of recombinant BioHe at 5-10 mM
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0.25
4-nitrophenyl caproate
pH 7.5, 37°C
0.29
p-nitrophenyl acetate
+/- 0.04
0.33
p-nitrophenyl butyrate
+/- 0.06
0.25
p-nitrophenyl caproate
+/- 0.02
0.6
p-nitrophenyl laurate
+/- 0.13
0.35
p-nitrophenyl propionate
+/- 0.08
0.25
1-naphthyl acetate
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0.29
4-nitrophenyl acetate
pH 7.5, 37°C
0.33
4-nitrophenyl butyrate
pH 7.5, 37°C
0.6
4-nitrophenyl laurate
pH 7.5, 37°C
0.35
4-nitrophenyl propionate
pH 7.5, 37°C
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18.5
4-nitrophenyl acetate
pH 7.5, 37°C
6.1
4-nitrophenyl butyrate
pH 7.5, 37°C
4
4-nitrophenyl caproate
pH 7.5, 37°C
1.5
4-nitrophenyl laurate
pH 7.5, 37°C
13.1
4-nitrophenyl propionate
pH 7.5, 37°C
18.5
p-nitrophenyl acetate
+/- 1.7
6.1
p-nitrophenyl butyrate
+/- 0.7
4
p-nitrophenyl caproate
+/- 0.1
1.5
p-nitrophenyl laurate
+/- 0.2
13.1
p-nitrophenyl propionate
+/- 1.2
18.5
4-nitrophenyl acetate
pH 7.5, 37°C
6.1
4-nitrophenyl butyrate
pH 7.5, 37°C
4
4-nitrophenyl caproate
pH 7.5, 37°C
1.5
4-nitrophenyl laurate
pH 7.5, 37°C
13.1
4-nitrophenyl propionate
pH 7.5, 37°C
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0.15
Phenylmethylsulfonylfluoride
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0.19
+/- 0.02, palmitoyl-CoA
12.7
+/- 1.5, p-nitrophenyl butyrate
27.5
+/- 2.5, p-nitrophenyl propionate
3.17
+/- 0.34, p-nitrophenyl laurate
38.9
+/- 3.6, p-nitrophenyl acetate
8.4
+/- 0.27, p-nitrophenyl caproate
additional information
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7 - 9
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90% of maximal activity within this range
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4 - 10
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activity profile, inactive at pH 3.0, overview
6 - 8.5
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pH 6.0: about 30% of maximal activity, pH 8.5: about 40% of maximal cativity
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15 - 60
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activity profile, overview
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SwissProt
brenda
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additional information
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BioHe also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway
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29152
x * 29152, mass spectrometry
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x * 29152, mass spectrometry
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purified recombinant enzyme, by hanging drop vapour diffusion method, 0.002 ml of each, protein solution and precipitant solution, equilibration against reservoir solution containing 1.2 M sodium citrate trihydrate and 0.1 M Tris-HCl, pH 8.0, 21°C, 2-5 days, X-ray diffraction structure determination at 1.7 A resolution, structure analysis
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3.5
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50% activity remaining after 1 h
709496
4
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30 min, 80% loss of activity
170987
5
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unstable below
170987
5 - 10
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completely stable after 1 h
709496
6 - 10
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30 min, stable
170987
3
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30 min, complete inactivation
170987
3
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inactivation after 1 h
709496
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55
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30 min, purified recombinant enzyme, more than 95% activity of BioHe remaining at 55°C
60
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10 min, 50% loss of activity
70
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10 min, complete loss of activity
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4°C, 5% glycerol, 0.5 M NaCl, no loss in activity after several months
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
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expression of the selenomethionine enriched enzyme in Escherichia coli methionine auxotroph strain B834 (DE3) in supplemented M9 medium
gene bioHe, DNA and amino acid sequence determination and analysis, sequence compariosns, overview
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Goullet, P.; Picard, B.; Laget, P.F.
Purification and properties of carboxylesterase B of Escherichia coli
Ann. Microbiol.
135A
375-387
1984
Escherichia coli, Escherichia coli HB17
brenda
Sanishvili, R.; Yakunin, A.F.; Laskowski, R.A.; Skarina, T.; Evdokimova, E.; Doherty-Kirby, A.; Lajoie, G.A.; Thornton, J.M.; Arrowsmith, C.H.; Savchenko, A.; Joachimiak, A.; Edwards, A.M.
Integrating structure, bioinformatics, and enzymology to discover function. BioH, a new carboxylesterase from Escherichia coli
J. Biol. Chem.
278
26039-26045
2003
Escherichia coli, Escherichia coli (P13001)
brenda
Kuznetsova, E.; Proudfoot, M.; Sanders, S.A.; Reinking, J.; Savchenko, A.; Arrowsmith, C.H.; Edwards, A.M.; Yakunin, A.F.
Enzyme genomics: Application of general enzymatic screens to discover new enzymes
FEMS Microbiol. Rev.
29
263-279
2005
Escherichia coli (P04335)
brenda
Kwon, M.A.; Kim, H.S.; Oh, J.Y.; Song, B.K.; Song, J.K.
Gene cloning, expression, and characterization of a new carboxylesterase from Serratia sp. SES-01: comparison with Escherichia coli BioHe enzyme
J. Microbiol. Biotechnol.
19
147-154
2009
Escherichia coli, Serratia sp. (B0M0H6), Serratia sp. SES-01 (B0M0H6)
brenda
Transporter Classification Database (TCDB):
1.B.12.5.9