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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Oryctolagus cuniculus and UniProt Accession P12337
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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: Oryctolagus cuniculus
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
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
-
-
-
-
CES
-
-
-
-
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
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
-
-
-
?
irinotecan + H2O
7-ethyl-10-hydroxycampothecin + 1,4'-bipiperidine-1'-carboxylic acid
antitumor prodrug, poor substrate
-
-
?
(+/-)-3-endo-acetyloxy-1,8-cineole + H2O
(1S,3S,4R)-(+)-3-acetyloxy-1,8-cineole + (1R,3R,4S)-(-)-3-hydroxy-1,8-cineole
-
-
-
-
?
(1RS)-cis-permethrin + H2O
cis-dichlorochrysamthemic acid + 3-phenoxybenzyl alcohol
-
-
-
-
?
(1RS)-trans-permethrin + H2O
trans-dichlorochrysamthemic acid + 3-phenoxybenzyl alcohol
-
-
-
-
?
2'-ethylcarbonate-linked paclitaxel + H2O
paclitaxel + propanoate
-
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
clopidogrel + H2O
(2S)-(2-chlorophenyl)(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)ethanoic acid + methanol
CPT-11 + H2O
SN-38 + 1,4'-bipiperidine-1'-carboxylic acid + CO2
-
-
-
-
?
O-butyryl propranolol + H2O
butanoate + propranolol
-
preferential hydrolysis of R-isomer by liver and intestine enzyme, non-enantioselective
-
-
?
additional information
?
-
-
carboxylesterases are enzymes that hydrolyze a broad suite of endogenous and exogenous ester-containing compounds to the corresponding alcohol and carboxylic acid
-
-
?
clopidogrel + H2O
(2S)-(2-chlorophenyl)(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)ethanoic acid + methanol
-
-
-
-
?
clopidogrel + H2O
(2S)-(2-chlorophenyl)(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)ethanoic acid + methanol
-
an anti-thrombogenic agent
-
-
?
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
clopidogrel + H2O
(2S)-(2-chlorophenyl)(6,7-dihydrothieno[3,2-c]pyridin-5(4H)-yl)ethanoic acid + methanol
-
an anti-thrombogenic agent
-
-
?
additional information
?
-
-
carboxylesterases are enzymes that hydrolyze a broad suite of endogenous and exogenous ester-containing compounds to the corresponding alcohol and carboxylic acid
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1,1,-trifluoro-3-(hexylsulfinyl)propane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
1,1,1,-trifluoro-3-(hexylsulfonyl)propane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
1,1,1-trifluoro-3-(hexyloxy)propane-2,2-diol1,1,1-trifluoro-3-(hexylsulfonyl)propane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
1,1,1-trifluoro-3-(octylsulfinyl)propane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
1,2-bis(2,3,4-trifluorophenyl)ethane-1,2-dione
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(2,3,5-trifluorophenyl)ethane-1,2-dione
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(2,3-difluorophenyl)ethane-1,2-dione
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(2,5-difluorophenyl)-2-hydroxyethanone
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(2,6-difluorophenyl)-2-hydroxyethanone
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(3,5-difluorophenyl)-2-hydroxyethanone
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(3,5-difluorophenyl)ethane-1,2-dione
comparison with inhibition of human isoforms hCE1 and hCE2
1,2-bis(4-fluorophenyl)ethane-1,2-dione
comparison with inhibition of human isoforms hCE1 and hCE2
2-hydroxy-1,2-bis(2,3,4-trifluorophenyl)ethanone
comparison with inhibition of human isoforms hCE1 and hCE2
2-hydroxy-1,2-bis(2,3,5-trifluorophenyl)ethanone
comparison with inhibition of human isoforms hCE1 and hCE2
3-butylsulfinyl-1,1,1-trifluoropropane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
3-decylsulfinyl-1,1,1-trifluoropropane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
3-decylsulfonyl-1,1,1-trifluoropropane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
3-dodecylsulfinyl-1,1,1-trifluoropropane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
3-dodecylsulfonyl-1,1,1-trifluoropropane-2,2-diol
comparison with inhibition of human isoforms hiCE and hCE1
benzil
comparison with inhibition of human isoforms hCE1 and hCE2
1,1'-ethane-1,2-diylbis(1H-indole-2,3-dione)
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-(2-bromoethyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-(2-iodoethyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-(4-(4[(2,3-dioxo-2,3-dihydro-1H-indol-1-yl)methyl]benzyl)benzyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-(4-chlorobenzyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-([(2-bromophenyl)amino]methyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-([(4-chlorophenyl)amino]methyl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-benzyl-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-dodecyl-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-hexadecyl-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-phenyl-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
1-[(2-naphthylamino)methyl]-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
2-chloro-3,4-dimethoxybenzil
-
blocks hydrolysis of trans-permethrin by isoform hCE2 36 times more efficiently than hCE1
4,6-dichloro-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
4,7-dichloro-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
5-bromo-1-(2-methylprop-2-en-1-yl)-1H-indole-2,3-dione
-
comparison with inhibition of human carboxyesterases hCE1 and hiCE and with acetyl- and butyrylcholinesterase
additional information
-
not inhibited by bis(p-nitrophenyl) phosphate
-
additional information
-
several different scaffolds capable of inhibiting carboxylesterases are e.g. organophosphates, carbamates, trifluoromethyl ketone-containing structures, and aromatic ethane-1,2-diones. Comparison of diverse benzil analogues and dione-based and trifluoromethyl ketone carboxylesterase inhibitors in carboxylesterase inhibition using classical and 3D-quantitative structure-activity relationship analysis, overview
-
additional information
-
not inhibited by butane-2,3-dione, hexane 3,4-dione, oxanilide, S1,S2-diphenyl ethane bis(thioate), diphenyl ethanedioate, 1,4-diphenylbutane-2,3-dione, and 1-bromo-1,4-diphenyl butane-2,3-dione
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000217
1,1,1,-trifluoro-3-(hexylsulfinyl)propane-2,2-diol
pH 7.4
0.0000343
1,1,1,-trifluoro-3-(hexylsulfonyl)propane-2,2-diol
pH 7.4
0.0000017
1,1,1-trifluoro-3-(hexyloxy)propane-2,2-diol1,1,1-trifluoro-3-(hexylsulfonyl)propane-2,2-diol
pH 7.4
0.0000064
1,1,1-trifluoro-3-(octylsulfinyl)propane-2,2-diol
pH 7.4
0.0001373
3-butylsulfinyl-1,1,1-trifluoropropane-2,2-diol
pH 7.4
0.0000016
3-decylsulfonyl-1,1,1-trifluoropropane-2,2-diol
pH 7.4
0.0000014
3-dodecylsulfinyl-1,1,1-trifluoropropane-2,2-diol
pH 7.4
0.0000007
3-dodecylsulfonyl-1,1,1-trifluoropropane-2,2-diol
pH 7.4
0.000027
1,2-dicyclohexylethane-1,2-dione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.0000205
1,4-dibromo-1,4-diphenyl butane-2,3-dione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.000006
1-(4-(4[(2,3-dioxo-2,3-dihydro-1H-indol-1-yl)methyl]benzyl)benzyl)-1H-indole-2,3-dione
-
-
0.0000065
hexadecane-8,9-dione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.000009
octadecane-9,10-dione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.00011
phenyl-1,2-heptanedione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.000337
phenyl-1,2-hexanedione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.0000281
phenyl-1,2-octanedione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.00271
phenyl-1,2-pentanedione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.004493
phenyl-1,2-propanedione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
0.0000151
tetradecane-7,8-dione
-
in 50 mM HEPES buffer, pH 7.4, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 5.0: about 55% of maximal activity, pH 10.0: about 75% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
comparison of hydrolytic activites with those of human, rabbits, monkeys, and dogs
-
comparison of hydrolytic activites with those of human, rabbits, monkeys, and dogs
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
carboxylesterases are involved in lipid homeostasis, including cholesterol metabolism and transport with a proposed role in the development of atherosclerosis
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). EST1_RABIT
565
0
62292
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the monomeric carboxylesterase is not a subunit of the oligomeric carboxylesterase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
the monomeric enzyme form contains 3.3% carbohydrate, the trimeric enzyme form contains 6.9% carbohydrate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of istatin analogue inhibitors into crystal structure of isoform hCE1
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isolation of mutant enzyme hCE1m6, which is 70fold more efficient in cleavage of the antitumor prodrug irinotecan-7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin, i.e. CPT-11, than wild-type
additional information
-
isolation of mutant enzyme hCE1m6, which is 70fold more efficient in cleavage of the antitumor prodrug irinotecan-7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin, i.e. CPT-11, than wild-type
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
isolation of mutant enzyme hCE1m6, which is 70fold more efficient in cleavage of the antitumor prodrug irinotecan-7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin, i.e. CPT-11, than wild-type. Adenoviral-mediated delivery of mutant enzyme with human tumor cells results in up to 670fold reduction in the IC50 value for CPT-11
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, M.; Lio, T.; Tabata, T.
Purification and characterization of a carboxylesterase from rabbit liver lysosomes
J. Biochem.
101
619-624
1987
Oryctolagus cuniculus
Miller, S.K.; Main, A.R.; Rush, R.S.
Purification and physical properties of oligomeric and monomeric carboxylesterases from rabbit liver
J. Biol. Chem.
255
7161-7167
1980
Oryctolagus cuniculus
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
Hicks, L.D.; Hyatt, J.L.; Moak, T.; Edwards, C.C.; Tsurkan, L.; Wierdl, M.; Ferreira, A.M.; Wadkins, R.M.; Potter, P.M.
Analysis of the inhibition of mammalian carboxylesterases by novel fluorobenzoins and fluorobenzils
Bioorg. Med. Chem.
15
3801-3817
2007
Homo sapiens (O00748), Homo sapiens (P23141), Oryctolagus cuniculus (P12337)
Wierdl, M.; Tsurkan, L.; Hyatt, J.L.; Edwards, C.C.; Hatfield, M.J.; Morton, C.L.; Houghton, P.J.; Danks, M.K.; Redinbo, M.R.; Potter, P.M.
An improved human carboxylesterase for enzyme/prodrug therapy with CPT-11
Cancer Gene Ther.
15
183-192
2008
Oryctolagus cuniculus (P12337), Oryctolagus cuniculus, Homo sapiens (P23141), Homo sapiens
Hyatt, J.L.; Moak, T.; Hatfield, M.J.; Tsurkan, L.; Edwards, C.C.; Wierdl, M.; Danks, M.K.; Wadkins, R.M.; Potter, P.M.
Selective inhibition of carboxylesterases by isatins, indole-2,3-diones
J. Med. Chem.
50
1876-1885
2007
Oryctolagus cuniculus, Homo sapiens (P23141)
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
Wadkins, R.M.; Hyatt, J.L.; Edwards, C.C.; Tsurkan, L.; Redinbo, M.R.; Wheelock, C.E.; Jones, P.D.; Hammock, B.D.; Potter, P.M.
Analysis of mammalian carboxylesterase inhibition by trifluoromethylketone-containing compounds
Mol. Pharmacol.
71
713-723
2007
Homo sapiens (O00748), Homo sapiens (P23141), Homo sapiens, Oryctolagus cuniculus (P12337)
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
Harada, T.; Nakagawa, Y.; Wadkins, R.M.; Potter, P.M.; Wheelock, C.E.
Comparison of benzil and trifluoromethyl ketone (TFK)-mediated carboxylesterase inhibition using classical and 3D-quantitative structure-activity relationship analysis
Bioorg. Med. Chem.
17
149-164
2009
Oryctolagus cuniculus, Homo sapiens
Parkinson, E.I.; Jason Hatfield, M.; Tsurkan, L.; Hyatt, J.L.; Edwards, C.C.; Hicks, L.D.; Yan, B.; Potter, P.M.
Requirements for mammalian carboxylesterase inhibition by substituted ethane-1,2-diones
Bioorg. Med. Chem.
19
4635-4643
2011
Oryctolagus cuniculus, Homo sapiens
EXTERNAL LINKS (specific for EC-Number 3.1.1.1)
Transporter Classification Database (TCDB): 1.B.12.5.9
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