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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Rattus norvegicus and UniProt Accession Q63108
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EC Tree
3.1.1.1 carboxylesteraseIUBMB 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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Word Map
- 3.1.1.1
- lipase
-
insecticide
- leukocyte
- lymphocyte
-
alpha-naphthyl
- leukemia
-
cytochemical
- urine
- isozymes
- p-nitrophenyl
-
organophosphate
-
prodrugs
-
ache
- phagocytic
- marrow
- urinary
-
organophosphorus
- hydrolases
-
pesticide
- lysosomal
- fluoride
- myeloid
- granulocyte
-
lipolytic
-
pyrethroids
- nitrite
-
neurotoxic
- paraoxon
-
phagocytosis
- carbamate
- mosquito
- chlorpyrifos
- paraoxonase
- histiocytic
-
urinalysis
-
cytochemistry
- kallikreins
- culex
- irinotecan
- dfp
- fluorophosphate
- diptera
-
diisopropyl
-
myelomonocytic
- pmsf
- soman
- parathion
-
allozymes
- diisopropylfluorophosphate
- oseltamivir
- industry
- environmental protection
- agriculture
- analysis
- diagnostics
- synthesis
- degradation
- biotechnology
- medicine
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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-5C
-
-
-
-
carboxylic acid esterase
-
-
-
-
carboxylic ester hydrolase
-
-
-
-
carboxylic esterase
-
-
-
-
Carboxylic-ester hydrolase
-
-
-
-
CES
CES1
CES2
cocaine esterase
-
-
-
-
Egasyn
-
-
-
-
Es-22
-
-
-
-
ES-HTEL
-
-
-
-
ES-HVEL
-
-
-
-
ES-Male
-
-
-
-
ES-THET
-
-
-
-
ES10
ES4
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
-
-
-
-
CES
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a carboxylic ester + H2O = an alcohol + a carboxylate
a catalytic triad is formed by residues Ser221, Glu353, and His466
a carboxylic ester + H2O = an alcohol + a carboxylate
a catalytic triad is formed by residues Ser224, Glu341, and His452
a carboxylic ester + H2O = an alcohol + a carboxylate
a catalytic triad is formed by residues Ser227, Glu344, and His456
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
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
9016-18-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
retinyl palmitate + H2O
retinol + palmitate
-
-
-
?
(1RS)-cis-permethrin + H2O
cis-dichlorochrysamthemic acid + 3-phenoxybenzyl alcohol
-
-
-
-
?
(1RS)-trans-permethrin + H2O
trans-dichlorochrysamthemic acid + 3-phenoxybenzyl alcohol
-
-
-
-
?
(S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone + H2O
(2S)-6-fluoro-2-methyl-1,2,3,4-tetrahydroquinoline + (isoquinolin-5-yloxy)acetic acid
1-monolauroyl-glycerol + H2O
lauric acid + glycerol
-
10.0% of the activity with tributyrin
-
-
?
1-monomyristoyl-glycerol + H2O
myristic acid + glycerol
-
11.6% of the activity with tributyrin
-
-
?
1-monopalmitin + H2O
palmitic acid + glycerol
-
3.8% of the activity with tributyrin
-
-
?
1-monostearin + H2O
stearic acid + glycerol
-
1.6% of the activity with tributyrin
-
-
?
2'-ethylcarbonate-linked paclitaxel + H2O
paclitaxel + propanoate
-
-
-
-
?
2-monopalmitin + H2O
palmitic acid + glycerol
-
2.6% of the activity with tributyrin
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
CPT-11 + H2O
SN-38 + ?
-
the substrate is more specific for isozyme CES2 than for CES1
-
-
?
delapril + H2O
N-[(1S)-1-carboxy-3-phenylpropyl]-L-alanyl-N-(2,3-dihydro-1H-inden-2-yl)glycine + ethanol
-
-
-
-
?
derapril + H2O
N-[(1S)-1-carboxy-3-phenylpropyl]-L-alanyl-N-(2,3-dihydro-1H-inden-2-yl)glycine + ethanol
-
-
-
-
?
heroin + H2O
6-monoacetylmorphine + acetate
-
the substrate is more specific for isozyme CES2 than for CES1
-
-
?
methylprednisolone 21-hemisuccinate + H2O
?
-
the substrate is more specific for isozyme CES2 than for CES1
-
-
?
N-acetyl-DL-phenylalanine beta-naphthyl ester + H2O
N-acetyl-DL-phenylalanine + beta-naphthol
NAPBNE, a chromogenic substrate of chymotrypsin-like enzymes
-
-
?
O-butyryl propranolol + H2O
butanoate + propranolol
-
preferential hydrolysis of S-isomer by liver enzyme
-
-
?
pranlukast + H2O
?
-
effectively hydrolyzed by carboxylesterase pI 6.2 but not by the pI 6.0 enzyme
-
-
?
tricaproin + H2O
caproic acid + glycerol
-
19.2% of the activity with tributyrin
-
-
?
tricaprylin + H2O
caprylic acid + glycerol
-
8.1% of the activity with tributyrin
-
-
?
(S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone + H2O
(2S)-6-fluoro-2-methyl-1,2,3,4-tetrahydroquinoline + (isoquinolin-5-yloxy)acetic acid
-
-
-
-
?
(S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone + H2O
(2S)-6-fluoro-2-methyl-1,2,3,4-tetrahydroquinoline + (isoquinolin-5-yloxy)acetic acid
-
cleavage of the amide bond, inhibited by bis(p-nitrophenyl) phosphate
-
-
?
1-monocaprylylglycerol + H2O
caprylic acid + glycerol
-
27% of the activity with tributyrin
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
specific substrate for isozyme CES1
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
the substrate is more specific for isozyme CES2 than for CES1
-
-
?
imidapril + H2O
?
-
the substrate is more specific for isozyme CES2 than for CES1
-
-
?
retinyl palmitate + H2O
retinol + palmitate
-
-
-
?
retinyl palmitate + H2O
retinol + palmitate
-
-
?
additional information
?
-
O35535
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
poor substrate: deltamethrin, esfenvalerate, alpha-cypermethrin, cis-permethrin
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone + H2O
(2S)-6-fluoro-2-methyl-1,2,3,4-tetrahydroquinoline + (isoquinolin-5-yloxy)acetic acid
-
-
-
-
?
additional information
?
-
O35535
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
additional information
?
-
phylogenetic tree for rat liver carboxylesterases
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-chloro-3,4-dimethoxybenzil
-
blocks hydrolysis of trans-permethrin by isoform hCE2 36 times more efficiently than hCE1
bis-p-nitrophenyl phosphate
O35535, O70177
BNPP, a specific inhibitor of CES, inhibits the hydrolysis of ethyl-FXD in rat skin S9 fraction in a dose-dependent manner, 99% inhibition at 1 mM BNPP
bis-4-nitrophenyl phosphate
O35535, O70177
BNPP, a specific inhibitor of CES, inhibits the hydrolysis of ethyl-FXD in rat skin S9 fraction in a dose-dependent manner, 99% inhibition at 1 mM BNPP
additional information
O35535
ethopropazine, a specific inhibitor of butyrylcholinesterase (EC 3.1.1.8), shows no inhibitory effect
-
additional information
ethopropazine, a specific inhibitor of butyrylcholinesterase (EC 3.1.1.8), shows no inhibitory effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00089
retinyl palmitate
isozyme ES3, pH 8.0, 37°C
0.0012
retinyl palmitate
isozyme ES10, pH 8.0, 37°C
0.0014
retinyl palmitate
isozyme ES4, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0032
retinyl palmitate
isozyme ES3, pH 8.0, 37°C
0.00083
retinyl palmitate
isozyme AB010635, pH 8.0, 37°C
0.0028 - 0.0045
retinyl palmitate
isozyme D50580, pH 8.0, 37°C
0.004
retinyl palmitate
isozyme ES10, pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16.7
purified isozyme ES4, substrate 4-methylumbelliferyl acetate
29.7
purified isozyme D50580, substrate 4-methylumbelliferyl acetate
30.1
purified isozyme ES3, substrate 4-methylumbelliferyl acetate
41.9
purified isozyme ES10, substrate 4-methylumbelliferyl acetate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
-
hydrolysis of methyl butyrate, at optimal methyl butyrate concentrations, 0.01 M
7.3
assay at, substrate 4-methylumbelliferyl acetate
7.4
7.5
-
hydrolysis of methyl hutyrate, at high substrate concentrations, 0.5 M
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
isozyme AB010635, isoelectric focusing
5.3
isozyme D50580, isoelectric focusing
5.7
isozyme ES3, isoelectric focusing
6
isozyme AY034877, isoelectric focusing
6.1
isozyme ES10, isoelectric focusing
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male Sprague-Dawley rat, isoenzyme ES3, belonging to the nonspecific carboxylesterase family
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the expression of the carboxylesterases ES4 and ES10 endothelial cells is 5-10fold lower than that in hepatocytes
additional information
-
comparison of hydrolytic activites with those of human, rabbits, monkeys, and dogs
-
comparison of hydrolytic activites with those of human, rabbits, monkeys, and dogs
-
CES2 but not CES1 is strongly expressed in small intestine
additional information
O35535
no isozyme expression in brain, thymus, heart, and spleen
additional information
no isozyme expression in brain, thymus, heart, and spleen
additional information
no isozyme expression in brain, thymus, heart, and spleen
additional information
no isozyme expression in brain, thymus, heart, and spleen
additional information
no isozyme expression in brain, thymus, heart, and spleen
additional information
no isozyme expression in brain, thymus, heart, and spleen
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EST1E_RAT
561
0
61715
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
62000
-
3 * 62000, mass spectrometry, deglycosylated enzyme, 3* 60300, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
trimer
trimer
-
3 * 62000, mass spectrometry, deglycosylated enzyme, 3* 60300, mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
glycoprotein
N-glycosylated residue is Asn275
glycoprotein
N-glycosylated residue is Asn79
glycoprotein
N-glycosylated residues are Asn261, Asn272, and Asn550
glycoprotein
N-glycosylated residues are Asn79 and Asn489
glycoprotein
N-glycosylated residues are Asn79, Asn107, and Asn489
glycoprotein
-
most CES isozymes are glycoproteins, and the carbohydrate chain is required for the enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.4
-
no degradation activity at pH 5.0, chemically stable at pH 6.0-7.4
691328
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme AB010635 from liver microsomes
isozyme AY034877 from liver microsomes
isozyme D50580 from liver microsomes
isozyme ES10 from liver microsomes
isozyme ES3 from liver microsomes
isozyme ES4 from liver microsomes
purification of the chymotrypsin-like enzyme from rat blood plasma by SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme with substrate (S)-1-(6-fluoro-2-methyl-3,4-dihydroquinolin-1(2H)-yl)-2-(isoquinolin-5-yloxy)ethanone and inhibitor bis(p-nitrophenyl) phosphate are useful in a system to measure in plasma-free fraction for a plasma-labile compound
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mentlein, R.; Schumann, M.; Heymann, E.
Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes
Arch. Biochem. Biophys.
234
612-621
1984
Rattus norvegicus
Abouakil, N.; Rogalska, E.; Bonicel, J.; Lombardo, D.
Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application of the human bile-salt-stimulated lipase
Biochim. Biophys. Acta
961
299-308
1988
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Tsujita, T.; Okuda, H.; Yamasaki, N.
Purification and some properties of carboxylesterase of rat adipose tissue
Biochim. Biophys. Acta
715
181-188
1982
Rattus norvegicus
Heymann, E.; Mentlein, R.
Carboxylesterases-amidases
Methods Enzymol.
77
333-344
1981
Rattus norvegicus
Hashinotsume, M.; Higashino, K.; Hada, T.; Yamamura, Y.
Purification and enzymatic properties of rat serum carboxylesterase
J. Biochem.
84
1325-1333
1978
Rattus norvegicus
Ikeda, Y.; Okamura, K.; Arima, T.; Fujii, S.
Purification and characterization of two types of esterase from rat liver microsomes
Biochim. Biophys. Acta
487
189-203
1977
Rattus norvegicus
Haugen, D.A.; Suttie, J.W.
Purification and properties of rat liver microsomal esterases
J. Biol. Chem.
249
2717-2722
1974
Rattus norvegicus
Arndt, R.; Heymann, E.; Junge, W.; Krisch, K.; Kollandt, H.
Purification and molecular properties of an unspecific carboxylesterase (E1) from rat-liver microsomes
Eur. J. Biochem.
36
120-128
1973
Rattus norvegicus
Arndt, R.; Krisch, K.
Catalytic properties of an unspecific carboxylesterase (E1) from rat-liver microsomes
Eur. J. Biochem.
36
129-134
1973
Rattus norvegicus
Mukherjee, J.J.; Jay, F.T.; Choy, P.C.
Purification, characterization and modulation of a microsomal carboxylesterase in rat liver for the hydrolysis of acyl-CoA
Biochem. J.
295
81-86
1993
Rattus norvegicus
Luan, L.; Sugiyama, T.; Takai, S; Usami, Y.; Adachi, T.; Katagiri, Y.; Hirano, K.
Purification and characterization of pranlukast hydrolase from rat liver microsomes: the hydrolase is identical to carboxylesterase pI 6.2
Biol. Pharm. Bull.
20
71-75
1997
Rattus norvegicus
Sanghani, S.P.; Davis, W.I.; Dumaual, N.G.; Mahrenholz, A.; Bosron, W.F.
Identification of microsomal rat liver carboxylesterases and their activity with retinyl palmitate
Eur. J. Biochem.
269
4387-4398
2002
Rattus norvegicus (O35535), Rattus norvegicus (O70631), Rattus norvegicus (P16303), Rattus norvegicus (Q63108), Rattus norvegicus (Q64573), Rattus norvegicus (Q8K3R0)
Linke, T.; Dawson, H.; Harrison, E.H.
Isolation and characterization of a microsomal acid retinyl ester hydrolase
J. Biol. Chem.
280
23287-23294
2005
Rattus norvegicus
Stocker, P.; Yousfi, M.; Djerridane, O.; Perrier, J.; Amziani, R.; El Boustani, S.; Moulin, A.
Effect of flavonoids from various Mediterranean plants on enzymatic activity of intestinal carboxylesterase
Biochimie
86
919-925
2004
Rattus norvegicus, Sus scrofa
Ross, M.K.; Borazjani, A.; Edwards, C.C.; Potter, P.M.
Hydrolytic metabolism of pyrethroids by human and other mammalian carboxylesterases
Biochem. Pharmacol.
71
657-669
2006
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Taketani, M.; Shii, M.; Ohura, K.; Ninomiya, S.; Imai, T.
Carboxylesterase in the liver and small intestine of experimental animals and human
Life Sci.
81
924-932
2007
Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Crow, J.A.; Borazjani, A.; Potter, P.M.; Ross, M.K.
Hydrolysis of pyrethroids by human and rat tissues: examination of intestinal, liver and serum carboxylesterases
Toxicol. Appl. Pharmacol.
221
1-12
2007
Homo sapiens, Rattus norvegicus (O70177)
Mello, T.; Nakatsuka, A.; Fears, S.; Davis, W.; Tsukamoto, H.; Bosron, W.F.; Sanghani, S.P.
Expression of carboxylesterase and lipase genes in rat liver cell-types
Biochem. Biophys. Res. Commun.
374
460-464
2008
Rattus norvegicus (O70631)
Tanino, T.; Nawa, A.; Miki, Y.; Iwaki, M.
Enzymatic stability of 2-ethylcarbonate-linked paclitaxel in serum and conversion to paclitaxel by rabbit liver carboxylesterase for use in prodrug/enzyme therapy
Biopharm. Drug Dispos.
29
259-269
2008
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Takahashi, S.; Katoh, M.; Saitoh, T.; Nakajima, M.; Yokoi, T.
Allosteric kinetics of human carboxylesterase 1: species differences and interindividual variability
J. Pharm. Sci.
97
5434-5445
2008
Rattus norvegicus, Homo sapiens (P23141), Homo sapiens
Hosokawa, M.
Structure and catalytic properties of carboxylesterase isozymes involved in metabolic activation of prodrugs
Molecules
13
412-431
2008
Canis lupus familiaris, Cavia porcellus, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Homo sapiens (P23141), Homo sapiens
Eng, H.; Niosi, M.; McDonald, T.S.; Wolford, A.; Chen, Y.; Simila, S.T.; Bauman, J.N.; Warmus, J.; Kalgutkar, A.S.
Utility of the carboxylesterase inhibitor bis-para-nitrophenylphosphate (BNPP) in the plasma unbound fraction determination for a hydrolytically unstable amide derivative and agonist of the TGR5 receptor
Xenobiotica
40
369-380
2010
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Lamego, J.; Coroadinha, A.S.; Simplicio, A.L.
Detection and quantification of carboxylesterase 2 activity by capillary electrophoresis
Anal. Chem.
83
881-887
2011
Bos taurus, Canis lupus familiaris, Equus caballus, Felis catus, Homo sapiens, Rattus norvegicus
Imai, T.; Ariyoshi, S.; Ohura, K.; Sawada, T.; Nakada, Y.
Expression of carboxylesterase isozymes and their role in the behavior of a fexofenadine prodrug in rat skin
J. Pharm. Sci.
105
714-721
2016
Rattus norvegicus (O35535), Rattus norvegicus (O70177), Rattus norvegicus Wistar (O35535), Rattus norvegicus Wistar (O70177)
Igetei, J.E.; Liddell, S.; El-Faham, M.; Doenhoff, M.J.
Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase
Parasitology
143
646-657
2016
Rattus norvegicus (P10959), Mus musculus (P23953), Mus musculus
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Transporter Classification Database (TCDB): 1.B.12.5.9
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