Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.1.1.1: carboxylesterase

This is an abbreviated version!
For detailed information about carboxylesterase, go to the full flat file.

Word Map on EC 3.1.1.1

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

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.1 carboxylesterase

Crystallization

Crystallization on EC 3.1.1.1 - carboxylesterase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with inhibitor paraoxon. Enzyme is a member of the alpha/beta hydrolase superfamily. Conserved catalytic triad residues are S169, D276, and H306, in the native structure, S169 has a three-carbon acyl adduct bound. Inhibitor paraoxon binds covalently to the catalytic serine resiude
hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A)
double-mutant M211S/R215L with bound inhibitor 1-hexadecanesulfonyl chloride, hanging drop vapour diffusion method, equal volumes of protein-inhibitor solution and reservoir solution, the latter containing 2 M ammonium sulfate, 0.1 M Tris buffer, pH 8.5, 2 weeks, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
crystals diffract to 2.8 A and belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 A
-
enzyme complexed with a sulfonyl derivative, X-ray diffraction structure determination and analysis at resolution 2.2 A
-
alignment studies show that enzyme has an alpha/beta hydrolase fold with catalytic triad formed by S190, E305, and H394
sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.2 M MgCl2, and 0.1 M Tris, pH 8.5
-
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
protein crystals are obtained at 20°C by vapor diffusion, crystal structure is determined at 1.5 A resolution
at 2.0 and 1.58 A resolution. Enzyme folds into a catalytic domain, an alpha/beta domain and a regulatory domain. Residue C408 adjacent to the active site is triply oxidized and may have a regulatory role
-
enzyme Est30, hanging drop vapour diffusion method, ammonium sulfate is used as a precipitant, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
carboxylesterase 1 in complex with cyclosarin, sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.3 M Li2SO4, 0.1 M citrate, pH 5.5, 0.1 M NaCl, 0.1 M LiCl, and 5% (v/v) glycerol.
-
covalent acyl-enzyme intermediate complexes of isoform hCE1 with inhibitors soman and tabun. Enzyme binds stereoselectively, (S)-stereoisomer of soman is preferred 10000fold over the (R)-isomer. Comparison with similar complexes of acetylcholinesterase
crystal structure of hCE1 in complex with the cocaine analogue homatropine to 2.8 A resolution, and with the heroin analogue naloxone to 2.9 A resolution
-
crystallized in the presence of either 10 mM naloxone methiodide or 100 mM homatropine using sitting drop vapor diffusion at 22°C. Overview of hCE1 structures, crystal structures of the hCE1 glycoprotein in complex with the cocaine analog homatropine and the heroin analog naloxone provide details about narcotic metabolism in humans. The hCE1 active site contains both specific and promiscuous compartments, which enable the enzyme to act on structurally distinct chemicals. A selective surface ligand-binding site regulates the trimer-hexamer equilibrium of hCE1 and allows each hCE1 monomer to bind two narcotic molecules simultaneously
in complex with coenzyme A, palmitate, cholate and taurocholate. Enzyme contains two additional ligand binding sites, each exhibiting relatively non-specific ligand binding properties. Catalytic triad is formed by residues S221, H468 and E354
-
molecular modeling of istatin analogue inhibitors into crystal structure of isoform hCE1
using a mixture consisting of 45% protein solution, 45% of condition No. 83 (2 M ammonium sulfate, 0.1 M bis-Tris pH 6.5, adjusted from pH 5.5) and 10% of condition No. 21 (2 M sodium thiocyanate)
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
molecular modeling of istatin analogue inhibitors into crystal structure of isoform hCE1
-
hanging drop vapor diffusion method, using PEGMME 5000 as precipitant
two crystal forms, form I in space group P21, resoöution 2.9A, form II, space group P21212, 2.1 A resolution
-
enzyme in complex with the inhibitor PMSF
-
hanging-drop vapor diffusion method, 1.6 A resolution
sitting drop vapor diffusion method, using 0.1 M HEPES/MOPS-Na, pH 7.5, 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350, 12.5% (v/v) 2-methyl-2,4-pentanediol, 0.03 M MgCl2, and 0.03 M CaCl2
-
protein crystals of wild-type enzyme and mutant enzyme Q249P/G250E are obtained at 20°C by vapor diffusion, crystal structure is determined at 1.5 A resolution
hanging-drop vapour diffusion method
sitting-drop vapor diffusion technique, the structures of R267E, R267G and R267K are highly similar to that of Sto-Est with only slight differences in atomic coordinates
purified recombinant wild-type enzyme NaM1, from 0.1 M MES, pH 8.5, with 25% w/v PEG 8000, X-ray diffraction structure determination and analysis at 2.03 A resolution, molecular replacement
-
at 2.1 A resolution. Enzyme exhibits a classical alpha/beta hydrolase fold with a central parallel-stranded beta sheet surrounded by alpha helices on both sides. The catalytic motif is formed by residues S154, D251, and H281. Enzyme forms a dimer via hydrophobic interactions through residues V274 and F276 on the beta strand off each monomer, and via salt bridges
-
sitting drop vapor diffusion method at 20°C, X-ray structures of the enzyme bound to a fatty acid and to its substrate acyl-homoserine lactone