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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Escherichia coli and UniProt Accession P04335

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.1 carboxylesterase
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.
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This record set is specific for:
Escherichia coli
UNIPROT: P04335
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACAT
-
-
-
-
Acyl coenzyme A:cholesterol acyltransferase
-
-
-
-
ali-esterase
-
-
-
-
aliesterase
-
-
-
-
alpha-carboxylesterase
-
-
-
-
B-esterase
-
-
-
-
Brain carboxylesterase hBr1
-
-
-
-
butyrate esterase
-
-
-
-
butyryl esterase
-
-
-
-
CaE
-
-
-
-
carboxyesterase
-
-
-
-
Carboxyesterase ES-10
-
-
-
-
carboxyl ester hydrolase
-
-
-
-
carboxylate esterase
-
-
-
-
carboxylesterase B
-
-
Carboxylesterase-5C
-
-
-
-
carboxylic acid esterase
-
-
-
-
carboxylic ester hydrolase
-
-
-
-
carboxylic esterase
-
-
-
-
Carboxylic-ester hydrolase
-
-
-
-
CES
-
-
-
-
cocaine esterase
-
-
-
-
Egasyn
-
-
-
-
Es-22
-
-
-
-
ES-HTEL
-
-
-
-
ES-HVEL
-
-
-
-
ES-Male
-
-
-
-
ES-THET
-
-
-
-
EST-5A
-
-
-
-
EST-5B
-
-
-
-
EST-5C
-
-
-
-
esterase A
-
-
-
-
esterase B
-
-
-
-
esterase D
-
-
-
-
esterase, carboxyl
-
-
-
-
Esterase-22
-
-
-
-
Esterase-31
-
-
-
-
HMSE
-
-
-
-
Kidney microsomal carboxylesterase
-
-
-
-
Liver microsomal carboxylesterase
-
-
-
-
methylbutyrase
-
-
-
-
methylbutyrate esterase
-
-
-
-
Microsomal palmitoyl-CoA hydrolase
-
-
-
-
monobutyrase
-
-
-
-
Monocyte/macrophage serine esterase
-
-
-
-
Non-specific carboxylesterase
-
-
-
-
nonspecific carboxylesterase
-
-
-
-
PI 5.5 esterase
-
-
-
-
PI 6.1 esterase
-
-
-
-
procaine esterase
-
-
-
-
Proline-beta-naphthylamidase
-
-
-
-
propionyl esterase
-
-
-
-
triacetin esterase
-
-
-
-
vitamin A esterase
-
-
-
-
additional information
-
the enzyme belongs to the BioH enzyme family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a carboxylic ester + H2O = an alcohol + a carboxylate
show the reaction diagram
active site structure, catalytic triad consists of residues Ser82, His235, and Asp207
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of esters
-
hydrolysis of carboxylic ester
-
-
-
-
hydrolysis of carboxylic or thio-esters
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9016-18-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
-
-
-
-
?
1-naphthyl butyrate + H2O
1-naphthol + butyrate
show the reaction diagram
-
-
-
-
?
1-naphthyl propionate + H2O
1-naphthol + propionate
show the reaction diagram
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
-
?
2-naphthyl butyrate + H2O
2-naphthol + butyrate
show the reaction diagram
-
-
-
-
?
2-naphthyl propionate + H2O
2-naphthol + propionate
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 caproate + H2O
4-nitrophenol + caproate
show the reaction diagram
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
?
p-nitrophenyl butyrate
p-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
p-nitrophenyl caprate
p-nitrophenol + caprate
show the reaction diagram
-
-
-
?
p-nitrophenyl caproate
p-nitrophenol + caproate
show the reaction diagram
-
-
-
?
p-nitrophenyl laurate
p-nitrophenol + laurate
show the reaction diagram
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
show the reaction diagram
-
-
-
?
p-nitrophenyl propionate
p-nitrophenol + propionate
show the reaction diagram
-
-
-
?
p-nitrophenyl stearate
p-nitrophenol + stearate
show the reaction diagram
-
-
-
?
palmitoyl-CoA
CoA + palmitate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHe is no metalloenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
-
62% inhibition of BioHe at 30%
2-mercaptoethanol
-
-
acetone
-
15% inhibition of BioHe at 30%
acetonitrile
-
89% inhibition of BioHe at 30%
ethanol
-
16% inhibition of BioHe at 30%
Fe2+
-
1 mM, 10% loss of activity
Hg2+
-
1 mM, 50% loss of activity
Isopropanol
-
70% inhibition of BioHe at 30%
methanol
-
7% inhibition of BioHe at 30%
Phenylmethylsulfonylfluoride
-
SDS
-
52% inhibition of recombinant BioHe at 0.2%
Zn2+
-
1 mM, 75% loss of activity
additional information
-
no inhibition by DMSO at 10-30%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
150% activation of recombinant BioHe at 5-10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
1-naphthyl acetate
-
-
0.29
4-nitrophenyl acetate
pH 7.5, 37°C
0.33
4-nitrophenyl butyrate
pH 7.5, 37°C
0.25
4-nitrophenyl caproate
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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.1
palmitoyl-CoA
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
Phenylmethylsulfonylfluoride
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
90% of maximal activity within this range
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
activity profile, inactive at pH 3.0, overview
6 - 8.5
-
pH 6.0: about 30% of maximal activity, pH 8.5: about 40% of maximal cativity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 60
-
activity profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
BioHe also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29152
x * 29152, mass spectrometry
57000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29152, mass spectrometry
monomer
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
50% activity remaining after 1 h
709496
4
-
30 min, 80% loss of activity
170987
5
-
unstable below
170987
5 - 10
-
completely stable after 1 h
709496
6 - 10
-
30 min, stable
170987
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
30 min, purified recombinant enzyme, more than 95% activity of BioHe remaining at 55°C
60
-
10 min, 50% loss of activity
70
-
10 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
4°C, 5% glycerol, 0.5 M NaCl, no loss in activity after several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team