3.1.1.1: carboxylesterase This is an abbreviated version! For detailed information about carboxylesterase, go to the full flat file .
Reaction
a carboxylic ester +
H2O =
an alcohol +
a carboxylate
Synonyms 4-nitrophenyl esterase, ACAT, Acetyl esterase, acetyl xylan esterase, acid retinyl ester hydrolase, AcXE, Acyl coenzyme A:cholesterol acyltransferase, acylcarnitine hydrolase, AF1716, AF1763, AFEST, ali-esterase, aliesterase, alpha-carboxylesterase, alpha-esterase 7, alphaE7, alphaEsterase7, AOPP herbicide carboxylesterase, APE1547, AREH, aspirin hydrolase, Axe1NaM1, Axe1NaM2, Axe1NaM3, B-esterase, Bacillus esterase, BdB1, BioHe, BioHs, Brain carboxylesterase hBr1, BSE, BsE-NP01, BSE01701, butyrate esterase, butyryl esterase, CaE, CaesCCR11, carboxyesterase, Carboxyesterase ES-10, carboxyl ester hydrolase, carboxyl esterase, carboxyl/cholinesterase, carboxylate esterase, carboxylesterase, carboxylesterase 1, carboxylesterase 1A2, carboxylesterase 1C, carboxylesterase 2, carboxylesterase B, carboxylesterase B1, carboxylesterase-1, carboxylesterase-2, Carboxylesterase-5C, carboxylic acid esterase, carboxylic ester hydrolase, carboxylic esterase, Carboxylic-ester hydrolase, CarE, CbE, CCE, CE, CE-1, CE-2, CE1, CE2, CE21p, CE7 AcXE, CEH, CES, CES 1C, CES-2, CES1, CES1-b, CES1-c, CES1A, CES1A1, CES1A2, Ces1c, Ces1d, Ces1e, Ces1g, CES2, CES2A1, Ces3-1, Ces3a, cholesteryl ester hydrolase, cocaine esterase, cocaine:benzoylecgonine esterase, COE, CPT-CE, CXE, CXE1, CXE10, D1CarE5, de-arenethiolase, DEHP, E3 carboxylesterase, E34Tt, EC 3.1.1.21, Egasyn, ES-10, Es-22, ES-HTEL, ES-HVEL, ES-Male, ES-THET, ES10, ES11, ES3, ES4, ES5, ES6, ES7, ES9, EST, EST-3, EST-4, EST-5A, EST-5B, EST-5C, Est-AF, Est0071, Est1, Est1C, EST2, ESt3, Est3 esterase, Est30, Est55, EstA, EstA esterase, EstB, estBB1, EstC, EstC1, esterase, esterase 1F, esterase 2, esterase 2B, esterase 6A, esterase 9A, esterase A, esterase B, esterase B1, esterase D, esterase Sso2518, esterase, carboxyl, Esterase-22, Esterase-31, esterase-6, EStFa, EstGtA2, EstP, EstPS1, EstSt7, EstU1, Fluazifop-P-butyl carboxylesterase, Fluazifop-P-butyl hydrolase, FpbH, fungus-inducible pepper carboxylesterase, general odorant degradation enzyme, GODE, hCE-2, HCE1, HCE2, hCES1, hiCE, HMSE, hormone-sensitive lipase, HSL, human carboxylesterase 1, human carboxylesterase 2, human liver carboxylesterase, ICE, ICXE14, JHE-related, JHER, kidney bean esterase, Kidney microsomal carboxylesterase, LcalphaE7, LIP4, LipA, LipC, Liver microsomal carboxylesterase, malathion carboxylesterase, MAP esterase, MCE, ME, MeIAA esterase, MeSA esterase, methylbutyrase, methylbutyrate esterase, mfCES2v3, Microsomal palmitoyl-CoA hydrolase, monobutyrase, Monocyte/macrophage serine esterase, More, mouse carboxylesterase, MT2282, NaM1, NaM2, NaM3, Non-specific carboxylesterase, nonspecific carboxylesterase, ODE, odorant degradation enzyme, P186_1588, PA3859, PepEST, PF2001, Pf2001 esterase, PI 5.5 esterase, PI 6.1 esterase, pig liver esterase, PLE, PMPMEase, pnbA, PnbA1, PnbA2, polyisoprenylated methylated protein methyl esterase, porcine liver carboxylesterase, PPE, PPMTase, PrbA, prenylated methylated protein methyl esterase, procaine esterase, Proline-beta-naphthylamidase, propionyl esterase, pyrethroid-hydrolysing esterase, Rsp3690, SABP2's methyl salicylate esterase, salicylic acid-binding protein 2, SeE, serine protease-like, serine-type carboxylesterase, SexiCXE10, SiRe0290, SshEstI, SshEstI esterase, Sso P1 carboxylesterase, Sso-EST1, SSO2493, SSO2517, SSoP1 CE, SsoPEst, ST0071, ST2026, STK_00710, Sto-Est, TGH, triacetin esterase, triacylglycerol hydrolase, vitamin A esterase, VmoLac
ECTree
Subunits
Subunits on EC 3.1.1.1 - carboxylesterase
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hexamer
trimer-hexamer equilibrium
homohexamer
-
6 * 35600, about, sequence calculation
?
x * 58000, SDS-PAGE
?
x * 57820, calculated from amino acid sequence
?
-
x * 58000, SDS-PAGE
-
?
-
x * 57820, calculated from amino acid sequence
-
?
-
x * 26000, SDS-PAGE
-
?
x * 28000, about, recombinant His-tagged enzyme, SDS-PAGE and sequence calculation
?
x * 52800, calculated from sequence
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
x * 28973, sequence calculation
?
-
x * 34000, SDS-PAGE of both isoforms CesA and CesB
?
x * about 32000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
?
-
x * 34000, SDS-PAGE of both isoforms CesA and CesB
-
?
-
x * about 32000, SDS-PAGE
-
?
-
x * 54000, SDS-PAGE
-
?
-
x * 34000, SDS-PAGE
-
?
-
x * 34000, SDS-PAGE of both isoforms CesA and CesB
-
?
Culex sp.
-
x * 62000, SDS-PAGE
?
x * 29152, mass spectrometry
?
-
x * 29000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 29000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 30000, SDS-PAGE
-
?
x * 27300, about, sequence calculation
?
-
x * 27300, about, sequence calculation
-
?
-
x * 50000, SDS-PAGE
-
?
x * 67500, SDS-PAGE, x * 67064, calculated, protein with S-tag
?
-
x * 67500, SDS-PAGE, x * 67064, calculated, protein with S-tag
-
?
-
x * 39800, predicted molecular mass for the N-terminal His6-tagged version of CXE1
?
x * 85000, about, SDS-PAGE
?
-
x * 31700, calculated
?
-
2 * 42100, calculated, His-tagged protein
?
x * 68000, about, enzyme without AT domain, sequence calculation
?
-
x * 68000, about, enzyme without AT domain, sequence calculation
-
?
x * 85000, about, SDS-PAGE
?
-
x * 33000, calculated from sequence
?
-
x * 33000, calculated from sequence
-
?
-
x * 58400, SDS-PAGE
-
?
-
x * 28300, SDS-PAGE
-
?
-
x * 64240, calculated from amino acid sequence
?
x * 40000, about, sequence calculation
?
-
x * 61380, sequence calculation
?
-
x * 60000, recombinant CXE10, SDS-PAGE
?
-
x * 61000, recombinant CXE10 calculated from amino acid sequence
?
x * 33810, calculated from sequence
?
x * 37000 (including a 3 kDa size increase by fusion tag), SDS-PAGE
?
x * 37400, calculated from sequence
?
-
x * 37000, SDS-PAGE
-
?
-
x * 37400, calculated from sequence
-
?
-
x * 33810, calculated from sequence
-
?
-
x * 37000 (including a 3 kDa size increase by fusion tag), SDS-PAGE
-
?
x * 34500, calculated, x * 35000, SDS-PAGE
?
-
x * 34500, calculated, x * 35000, SDS-PAGE
-
?
-
x * 40000, SDS-PAGE, x * 39313, calculated, His-tagged protein
?
-
x * 26000, about, sequence calculation
?
-
x * 35900, about, sequence calculation
?
-
x * 27528, calculated
?
-
x * 27528, calculated
-
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
-
dimer
-
2 * 72000, SDS-PAGE, gel filtration in presence of 8 M urea
dimer
-
Est30, 2 * 28338, calculated
dimer
-
2 * 35000, SDS-PAGE
dimer
2 * 29000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 29000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 30000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 30000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 27000, SDS-PAGE, both E1 and E2
dimer
-
2 * 27000, SDS-PAGE, both E1 and E2
-
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 28000, SDS-PAGE
-
dimer
2 * 30000, the crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. A temperature-dependent activation mechanism of the Pf2001 esterase is proposed via dimerization that is necessary for the substrate channel formation in the active site cleft
dimer
-
2 * 80000, esterase II, SDS-PAGE
dimer
-
and trimer, 2 *33000, calculated, 2 * 33000, SDS-PAGE
dimer
-
2 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE
dimer
-
and trimer, 2 *33000, calculated, 2 * 33000, SDS-PAGE
-
dimer
-
2 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE
-
dimer
2 * 33000, SDS-PAGE, recombinant enzyme expressed in Sulfolobus solfataricus, dimer
dimer
-
2 * 33000, SDS-PAGE, recombinant enzyme expressed in Sulfolobus solfataricus, dimer
-
dimer
R267 is important for the dimer integrity of Sto-Est that contributes to its overall stability
dimer
-
R267 is important for the dimer integrity of Sto-Est that contributes to its overall stability
-
dimer
2 * 37700, SDS-PAGE
dimer
-
crystallization data
homodimer
the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity
homodimer
-
the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity
-
homodimer
-
2 * 60000, SDS-PAGE
homotrimer
3 * 40000, SDS-PAGE
homotrimer
3 * 40400, calculated from sequence
homotrimer
-
3 * 40000, SDS-PAGE
-
homotrimer
-
3 * 40400, calculated from sequence
-
monomer
-
1 * 45000, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
-
monomer
-
1 * 36500, SDS-PAGE
monomer
-
1 * 27500, gel filtration
monomer
1 * 33800, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
-
monomer
-
1 * 60000, SDS-PAGE and MALDI-TOF
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 43000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 57100, SDS-PAGE
monomer
-
1 * 72800, SDS-PAGE
monomer
-
gel filtration
-
monomer
1 * 36000, SDS-PAGE
monomer
1 * 34734, calculated from sequence
monomer
-
1 * 50000, SDS-PAGE
monomer
-
Est55, 1 * 54867, calculated
monomer
-
1 * 20000, SDS-PAGE
monomer
-
1 * 61000, liver enzyme, SDS-PAGE
monomer
1 * 73000, SDS-PAGE
monomer
1 * 73000, SDS-PAGE, 1 * 73500, calculated
monomer
-
1 * 73000, SDS-PAGE
-
monomer
-
1 * 73000, SDS-PAGE, 1 * 73500, calculated
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
x * 54000, calculated
monomer
-
1 * 65300, SDS-PAGE
monomer
1 * 24000, SDS-PAGE
monomer
-
1 * 28000, SDS-PAGE, 1 * 24691, ESI-MS
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
1 * 42000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 42000, recombinant enzyme, SDS-PAGE
-
monomer
1 * 30000, the crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. A temperature-dependent activation mechanism of the Pf2001 esterase is proposed via dimerization that is necessary for the substrate channel formation in the active site cleft
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 70000, esterase I, SDS-PAGE
monomer
-
x * 61000, gel filtration
monomer
-
1 * 60000, isoenzyme pI 6.2, SDS-PAGE
monomer
-
1 * 63000, all isozymes, SDS-PAGE
monomer
-
1 * 16700, SDS-PAGE
monomer
-
1 * 16700, SDS-PAGE
-
monomer
1 * 35000, SDS-PAGE
monomer
-
1 * 34000, SDS-PAGE, MALDI-TOF
monomer
1 * 34260, calculated from sequence
monomer
-
1 * 34000, SDS-PAGE, MALDI-TOF
-
monomer
-
1 * 35000, SDS-PAGE
-
monomer
-
1 * 34260, calculated from sequence
-
monomer
protein exhibits activity even in the monomeric form
monomer
-
protein exhibits activity even in the monomeric form
-
monomer
-
1 * 45000, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
-
monomer
1 * 34000, SDS-PAGE
monomer
-
1 * 62000, about, both enzyme forms, SDS-PAGE
multimer
-
x * 42000, SDS-PAGE, x * 43300, calculated, His-tagged protein
multimer
-
x * 44000, SDS-PAGE, x * 42100, calculated, His-tagged protein
oligomer
-
n * 62000, SDS-PAGE
oligomer
-
n * 62000, SDS-PAGE
-
tetramer
-
4 * 85000, SDS-PAGE
tetramer
or higher oligomeric state, 4 * 69000, calculation from amino acid sequence
tetramer
-
or higher oligomeric state, 4 * 69000, calculation from amino acid sequence
-
tetramer
-
4 * 32000, SDS-PAGE
tetramer
-
4 * 33425, calculated from sequence
tetramer
-
4 * 32000, SDS-PAGE
-
tetramer
-
4 * 33425, calculated from sequence
-
tetramer
4 * 32000, SDS-PAGE
trimer
-
3 * 60000, SDS-PAGE
trimer
-
3 * 61500, SDS-PAGE
trimer
-
3 * 61000, liver enzyme, SDS-PAGE
trimer
-
3 * 59000, SDS-PAGE
trimer
trimer-hexamer equilibrium
trimer
-
3 * 60200, SDS-PAGE
trimer
-
3 * 30000, SDS-PAGE
trimer
-
3 * 70800, SDS-PAGE
trimer
-
3 * 58000, SDS-PAGE
trimer
3 * 33000, SDS-PAGE
trimer
-
3 * 33000, SDS-PAGE
-
trimer
3 * 34000, SDS-PAGE
trimer
3 * 34354, calculation from sequence
trimer
-
3 * 34000, SDS-PAGE
-
trimer
-
3 * 34354, calculation from sequence
-
trimer
-
3 * 65000, SDS-PAGE
trimer
-
3 * 58000, isoenzyme pI 6.0, SDS-PAGE
trimer
-
3 * 61500, SDS-PAGE
trimer
-
2 * 66000-72000, SDS-PAGE
trimer
-
3 * 62000, mass spectrometry, deglycosylated enzyme, 3* 60300, mass spectrometry
trimer
-
and drimer, 3 *33000, calculated, 3 * 33000, SDS-PAGE
trimer
-
3 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE
trimer
-
and drimer, 3 *33000, calculated, 3 * 33000, SDS-PAGE
-
trimer
-
3 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE
-
trimer
3 * 33428, calculated from sequence
trimer
-
3 * 33428, calculated from sequence
-
trimer
-
3 * 61000-62000, SDS-PAGE
trimer
-
3 * 63000, SDS-PAGE of glycosylated protein, 3 * 58000, SDS-PAGE of non-glycosylated protein. 3 * 61500, calculated
trimer
-
3 * 61000-62000, SDS-PAGE
-
additional information
-
N-terminal amino acid sequence is identical for E1 and E2
additional information
-
N-terminal amino acid sequence is identical for E1 and E2
-
additional information
-
the monomeric carboxylesterase is not a subunit of the oligomeric carboxylesterase
additional information
-
N-terminal amino acid sequence
additional information
-
the hexamer is composed of two trimers, each NaM1 monomer directly interacts with the two monomers from the same trimer and with two monomers from the opposite trimer