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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Lucilia cuprina and UniProt Accession Q25252

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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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Lucilia cuprina
UNIPROT: Q25252
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The taxonomic range for the selected organisms is: Lucilia cuprina
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
alpha-carboxylesterase
-
alpha-esterase 7
-
alphaEsterase7
-
E3 carboxylesterase
-
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-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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (1R,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1R,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2R)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (1R,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,2S,3S)-2-(2,2-dichloroethenyl)-3-methylcyclopropanecarboxylate + (2R)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (2R)-2-(4-chlorophenyl)-3-methylbutanoate + H2O
(2R)-2-(4-chlorophenyl)-3-methylbutanoic acid + (2R)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(R)-cyano(6-methoxynaphthalen-2-yl)methyl (2S)-2-(4-chlorophenyl)-3-methylbutanoate + H2O
(2S)-2-(4-chlorophenyl)-3-methylbutanoic acid + (2R)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(S)-cyano(6-methoxynaphthalen-2-yl)methyl (1R,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1R,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(S)-cyano(6-methoxynaphthalen-2-yl)methyl (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(S)-cyano(6-methoxynaphthalen-2-yl)methyl (1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(S)-cyano(6-methoxynaphthalen-2-yl)methyl (2R)-2-(4-chlorophenyl)-3-methylbutanoate + H2O
(2R)-2-(4-chlorophenyl)-3-methylbutanoic acid + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
(S)-cyano(6-methoxynaphthalen-2-yl)methyl (2S)-2-(4-chlorophenyl)-3-methylbutanoate + H2O
(2S)-2-(4-chlorophenyl)-3-methylbutanoic acid + (2S)-hydroxy(6-methoxynaphthalen-2-yl)ethanenitrile
show the reaction diagram
-
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
show the reaction diagram
-
-
-
?
diethyl-4-methylumbelliferyl phosphate + H2O
?
show the reaction diagram
-
-
-
?
methyl decanoate + H2O
methanol + decanoic acid
show the reaction diagram
-
-
-
?
methyl hexanoate + H2O
methanol + hexanoic acid
show the reaction diagram
-
-
-
?
methyl laurate + H2O
methanol + lauric acid
show the reaction diagram
-
-
-
?
methyl myristate + H2O
methanol + myristic acid
show the reaction diagram
-
-
-
?
methyl octanoate + H2O
methanol + octanoic acid
show the reaction diagram
-
-
-
?
3-phenoxybenzyl (1R,3R)-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1R,3R)-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropanecarboxylic acid + (3-phenoxyphenyl)methanol
show the reaction diagram
-
i.e. 1R-cis-NRDC157
-
-
?
3-phenoxybenzyl (1R,3S)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1R,3S)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylic acid + (3-phenoxyphenyl)methanol
show the reaction diagram
-
i.e. 1R-trans-permethrin, strong chiral preference for the 1S over the 1R isomers of permethrin
-
-
?
3-phenoxybenzyl (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylic acid + (3-phenoxyphenyl)methanol
show the reaction diagram
-
i.e. 1S-trans-permethrin, strong chiral preference for the 1S over the 1R isomers of permethrin
-
-
?
3-phenoxybenzyl (1S,3S)-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropanecarboxylate + H2O
(1S,3S)-3-(2,2-dibromovinyl)-2,2-dimethylcyclopropanecarboxylic acid + (3-phenoxyphenyl)methanol
show the reaction diagram
-
i.e. 1S-cis-NRDC157
-
-
?
additional information
?
-
dephosphorylation is the rate-limiting step in the hydrolysis of organophosphates by enzyme LcalphaE7
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1(R)-cis-alpha(S) deltamethrin
-
diethylumbelliferyl phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50
diethyl-4-methylumbelliferyl phosphate
in 25 mM Tris-HCl (pH 8.0), at 25°C
1380
methyl decanoate
in 25 mM Tris-HCl (pH 8.0), at 25°C
280
methyl hexanoate
in 25 mM Tris-HCl (pH 8.0), at 25°C
200
methyl laurate
in 25 mM Tris-HCl (pH 8.0), at 25°C
61
methyl myristate
in 25 mM Tris-HCl (pH 8.0), at 25°C
830
methyl octanoate
in 25 mM Tris-HCl (pH 8.0), at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme plays an important physiological role in lipid metabolism and is implicated in the detoxification of organophosphate insecticides
additional information
residues Phe100, Met147, and Tyr457 are located near the substrate-binding pocket, multi-conformer modeling of Tyr457. Kinetic analysis of the role of Tyr457 and Met147 reveals catalytic evidence for dynamic coupling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q25252_LUCCU
570
0
65416
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer or dimer
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
for investigation of binding-pocket heterogeneity, several previously published structures of enzyme LcalphaE7 in apostructure, with bound substrate and in phosphorylated form are re-processed to increase the amount of crystallographic data available, conformational selection upon substrate binding (PDB IDs are 5CH3, 5CH5, 5IVD, 5IVI, 5IVH, 5IVK, 4QWM, 4UBI, 4UBJ, 4UBK, 4UBM, 4UBL, 4UBN, 4UBO, 4W1Q, 4W1P, 4W1R, and 4W1S), overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M147A
site-directed mutagenesis, the mutant shows altered inhibition kinetics for inhibitor diethylumbelliferyl phosphate compared to wild-type enzyme
M364L/I419F/A472T/I505T/K530E/D554G
the mutant shows enhanced activity
W251L/D449G
the mutant shows a loss of activity for most substrates
W251L/D473N
the mutant shows a loss of activity for most substrates
W251L/I140F
the mutant shows a loss of activity for most substrates
W251L/I459N
the mutant shows a loss of activity for most substrates
W251L/R458C
the mutant shows a loss of activity for most substrates
W251L/R461H
the mutant shows a loss of activity for most substrates
W251L/R461S
the mutations result in improved activity
W251L/S462I
the mutant shows a loss of activity for most substrates
Y457A
site-directed mutagenesis, the mutant shows altered inhibition kinetics for inhibitor diethylumbelliferyl phosphate compared to wild-type enzyme
E217M
-
mutant in anionic site, p1 subsite, pyrethroid hydrolysis similar to wild-type
F309L
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis-substrate, strong increase for trans-substrate
F354L
-
mutant in anionic site, p1 subsite, pyrethroid hydrolysis similar to wild-type
F354W
-
mutant in anionic site, p1 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
G137D
-
mutant in oxyanion hole, marked decrease in pyrethroid hydrolysis
G137E
-
mutant in oxyanion hole, strong decrease in pyrethroid hydrolysis
G137H
-
mutant in oxyanion hole, marked decrease in pyrethroid hydrolysis
G137R
-
mutant in oxyanion hole, pyrethroid hydrolysis similar to wild-type
W251A
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
W251G
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
W251L
-
mutant in acyl pocket p2 subsite, strong increase in pyrethroid hydrolysis both for cis- and trans-substrate. Trans:cis ratio for preference of substrate is 2:1 compared to 27:1 in wild-type
W251L/F309L
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate. Trans:cis ratio for preference of substrate is 2:1 compared to 27:1 in wild-type
W251L/G137D
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate. Trans:cis ratio for preference of substrate is 2:1 compared to 27:1 in wild-type
W251L/P250S
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate. Trans:cis ratio for preference of substrate is 3:1 compared to 27:1 in wild-type
W251S
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
W251T
-
mutant in acyl pocket p2 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
Y148F
-
mutant in anionic site, p1 subsite, marked increase in pyrethroid hydrolysis both for cis- and trans-substrate
Y148F/G137D
-
marked decrease in pyrethroid hydrolysis, trans:cis ratio for preference of substrate is 87:1 compared to 24:1 in wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli JM109 and BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heidari, R.; Devonshire, A.L.; Campbell, B.E.; Dorrian, S.J.; Oakeshott, J.G.; Russell, R.J.
Hydrolysis of pyrethroids by carboxylesterases from Lucilia cuprina and Drosophila melanogaster with active sites modified by in vitro mutagenesis
Insect Biochem. Mol. Biol.
35
597-609
2005
Drosophila melanogaster, Lucilia cuprina
Manually annotated by BRENDA team
Coppin, C.W.; Jackson, C.J.; Sutherland, T.; Hart, P.J.; Devonshire, A.L.; Russell, R.J.; Oakeshott, J.G.
Testing the evolvability of an insect carboxylesterase for the detoxification of synthetic pyrethroid insecticides
Insect Biochem. Mol. Biol.
42
343-352
2012
Lucilia cuprina (Q25252), Lucilia cuprina
Manually annotated by BRENDA team
Jackson, C.J.; Liu, J.W.; Carr, P.D.; Younus, F.; Coppin, C.; Meirelles, T.; Lethier, M.; Pandey, G.; Ollis, D.L.; Russell, R.J.; Weik, M.; Oakeshott, J.G.
Structure and function of an insect alpha-carboxylesterase (alphaEsterase7) associated with insecticide resistance
Proc. Natl. Acad. Sci. USA
110
10177-10182
2013
Lucilia cuprina (Q25252)
Manually annotated by BRENDA team
Correy, G.J.; Carr, P.D.; Meirelles, T.; Mabbitt, P.D.; Fraser, N.J.; Weik, M.; Jackson, C.J.
Mapping the accessible conformational landscape of an insect carboxylesterase using conformational ensemble analysis and kinetic crystallography
Structure
24
977-987
2016
Lucilia cuprina (Q25252)
Manually annotated by BRENDA team