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Ligand Alpha-naphthyl acetate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.121

UDP-glucose + 1-naphthalene acetate = UDP + 1-naphthalene acetyl-beta-D-glucose

736956

-

3.1.1.1

1-naphthyl acetate + H2O = 1-naphthol + acetate

170987, 170979, 170981, 716812, 729255, 171026, 661545, 171017, 681338, 171004, 713766, 714004

-

3.1.1.1

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

693444, 692110

-

3.1.1.1

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

690570, 695077, 694067, 693646, 692471, 649399, 651506, 661545, 691913, 692617, 692622, 751792, 692111, 651507, 680782

-

3.1.1.1

3 entries

3.1.1.113

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

752538

-

3.1.1.2

1-naphthyl acetate + H2O = 1-naphthol + acetate

35195, 35199, 35203, 750166, 670481, 646527, 713914

-

3.1.1.2

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

653436, 670485, 692889, 708755

-

3.1.1.3

1-naphthyl acetate + H2O = 1-naphthol + acetate

714773, 730877

-

3.1.1.3

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

650660

-

3.1.1.41

1-naphthyl acetate + H2O = 1-naphthol + acetate

746975, 749261

-

3.1.1.41

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

170667

-

3.1.1.2

2 entries

3.1.1.3

2 entries

3.1.1.41

2 entries

3.1.1.45

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

671042

-

3.1.1.53

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

94419, 94408, 94410, 94417

-

3.1.1.53

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

653421

-

3.1.1.53

2 entries

3.1.1.55

1-naphthyl acetate + H2O = 1-naphthol + acetate

646021

-

3.1.1.56

1-naphthyl acetate + H2O = 1-naphthol + acetate

646032, 80990, 646036

-

3.1.1.59

1-naphthyl acetate + H2O = 1-naphthol + acetate

750396, 708700, 23487

-

3.1.1.59

alpha-naphthyl acetate + H2O = ?

651500

-

3.1.1.59

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

649497, 651510, 651512, 707525

-

3.1.1.6

1-naphthol acetate + H2O = 1-naphthol + acetate

35236, 35230, 23597, 35226

-

3.1.1.6

1-naphthyl acetate + H2O = 1-naphthol + acetate

653087, 730907, 678012, 680319, 750541

-

3.1.1.6

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

23594, 35241, 23600, 35223, 701417, 699069

-

3.1.1.7

1-naphthyl acetate + H2O = 1-naphthol + acetate

749984

-

3.1.1.7

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

682305

-

3.1.1.7

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

114133, 665325

-

3.1.1.72

1-naphthyl acetate + H2O = 1-naphthol + acetate

664203, 752117, 681094, 665786, 729438, 749664

-

3.1.1.72

1-naphthyl acetate + H2O = naphthol + acetate

23597

-

3.1.1.72

alpha-naphthyl acetate + H2O = 1-naphthol + acetate

664492

-

3.1.1.72

alpha-naphthyl acetate = acetate + 2-naphthol

23600, 23591

-

3.1.1.73

1-naphthyl acetate + H2O = 1-naphthol + acetate

741805

-

3.1.1.73

1-naphthyl acetate + H2O = 1-naphthol + acetic acid

737582

-

3.1.1.73

1-naphthyl acetate + H2O = acetic acid + 1-naphthol

208312, 208316, 208302, 208310, 699282

-

3.1.1.73

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

679997

-

3.1.1.79

1-naphthyl acetate + H2O = 1-naphthol + acetate

706584

-

3.1.1.79

alpha-naphtyl acetate + H2O = ?

706584

-

3.1.1.59

3 entries

3.1.1.6

3 entries

3.1.1.7

3 entries

3.1.1.72

4 entries

3.1.1.73

4 entries

3.1.1.79

2 entries

3.1.2.12

alpha-naphthyl acetate + H2O = alpha-naphthol + acetate

665750, 80990, 649455

-

3.2.1.72

alpha-naphthylacetate + H2O = alpha-naphthol + acetate

742766

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.53

competitive inhibitor

653421

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (36 results)

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Show Turnover Number (36 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.4.1.121

0.53

-

pH 7.6, 30°C

736956

3.1.1.1

1.8

-

malathion-specific enzyme, pH 6.9, 25°C

651507

3.1.1.1

4.8

-

in 2.5 mM Bicine buffer, pH 8.3, at 30°C

729255

3.1.1.1

11.6

-

pH 7.0, 25°C

681338

3.1.1.1

12.1

-

non-specific enzyme, pH 6.9, 25°C

651507

3.1.1.1

500

-

-

171017

3.1.1.1

3000

-

-

661545

3.1.1.1

3000

-

-

661545

3.1.1.1

7 entries

3.1.1.113

29

-

37°C, pH 7.5

752538

3.1.1.2

4.7

-

immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C

750166

3.1.1.2

450

-

recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C

692889

3.1.1.45

0.24

-

E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0

671042

3.1.1.45

1.6

-

E36D,C123S mutant enzyme, pH 7.0

671042

3.1.1.45

2.05

-

E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0

671042

3.1.1.45

63.4

-

C123S mutant enzyme, pH 7.0

671042

3.1.1.45

71.2

-

E36D,C123S mutant enzyme, pH 7.0

671042

3.1.1.45

86.2

-

E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0

671042

3.1.1.45

98.1

-

E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0

671042

3.1.1.45

120

-

C123S mutant enzyme, pH 7.0

671042

3.1.1.2

2 entries

3.1.1.45

8 entries

3.1.1.59

22

-

wild-type, at 30°C in 50 mM sodium phosphate buffer, pH 7.4, containing 1 mg/mL of bovine serum albumin

707525

3.1.1.72

0.53

-

substrate: alpha-naphthylacetate, wild-type enzyme

664203

3.1.1.72

60.5

-

substrate: alpha-naphthylacetate, mutant enzyme S146A

664203

3.1.1.72

81.9

-

substrate: alpha-naphthylacetate, wild-type enzyme

664203

3.1.1.72

131.3

-

substrate: alpha-naphthylacetate, mutant enzyme D168A

664203

3.1.1.72

411

-

substrate: alpha-naphthylacetate, mutant enzyme D168A

664203

3.1.1.73

2.75

-

20°C, pH 7.4

679997

3.1.1.73

32

-

pH 6.0, 55°C

737582, 741805

3.1.2.12

2.17

-

pH 8.0, 37°C, recombinant YeiG mutant D80A

665750

3.1.2.12

2.23

-

pH 8.0, 37°C, recombinant YeiG mutant D255A

665750

3.1.2.12

2.96

-

pH 8.0, 37°C, recombinant YeiG mutant D199A

665750

3.1.2.12

3.13

-

pH 8.0, 37°C, recombinant YeiG mutant D218A

665750

3.1.2.12

3.3

-

pH 8.0, 37°C, recombinant wild-type YeiG

665750

3.1.2.12

3.81

-

pH 8.0, 37°C, recombinant YeiG mutant D218A

665750

3.1.2.12

5.09

-

pH 8.0, 37°C, recombinant wild-type YeiG

665750

3.1.2.12

5.1

-

pH 8.0, 37°C, recombinant YeiG mutant C54A

665750

3.1.2.12

5.12

-

pH 8.0, 37°C, recombinant YeiG mutant C26A

665750

3.1.1.72

5 entries

3.1.1.73

2 entries

3.1.2.12

9 entries

K_M Value (53 results)

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Show KM Value (53 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.4.1.121

4

-

pH 7.6, 30°C

736956

3.1.1.1

0.00001

-

non-specific enzyme, pH 6.9, 25°C

651507

3.1.1.1

0.0001

-

malathion-specific enzyme, pH 6.9, 25°C

651507

3.1.1.1

0.008

-

-

171017

3.1.1.1

0.027

-

isozyme ME3, pH 7.0, 27°C

651506

3.1.1.1

0.048

-

isozyme ME2, pH 7.0, 27°C

651506

3.1.1.1

0.052

-

isozyme ME1, pH 7.0, 27°C

651506

3.1.1.1

0.131

-

-

171004

3.1.1.1

0.16

-

-

170979

3.1.1.1

0.222

-

at 25°C

692110

3.1.1.1

0.25

-

-

170987

3.1.1.1

0.37

-

-

170981

3.1.1.1

0.64

-

in 2.5 mM Bicine buffer, pH 8.3, at 30°C

729255

3.1.1.1

1.01

-

pH 7.0, 25°C

681338

3.1.1.1

13 entries

3.1.1.113

0.018

-

37°C, pH 7.5

752538

3.1.1.2

0.029

-

recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C

692889

3.1.1.2

0.039

-

immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C

750166

3.1.1.2

0.041

-

in 50 mM Tris-HCl (pH 8.0), at 37°C

713914

3.1.1.2

0.19

-

-

35203

3.1.1.45

0.02

-

E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0

671042

3.1.1.45

0.023

-

E36D,C123S mutant enzyme, pH 7.0

671042

3.1.1.45

0.032

-

E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0

671042

3.1.1.45

0.074

-

C123S mutant enzyme, pH 7.0

671042

3.1.1.2

4 entries

3.1.1.45

4 entries

3.1.1.53

1.71

-

pH 7.5, 37°C

653421

3.1.1.55

0.00043

-

pH 7.8, 25°C, isozyme I

646021

3.1.1.55

0.00078

-

pH 7.8, 25°C, isozyme II

646021

3.1.1.56

0.86

-

pH 7.0, 37°C

80990

3.1.1.56

2.5

-

pH 5.2, 37°C, isoenzyme Es D1

646032

3.1.1.56

3.1

-

pH 5.2, 37°C, isoenzyme Es D2

646032

3.1.1.59

0.12

-

-

651500

3.1.1.59

0.41

-

wild-type, at 30°C in 50 mM sodium phosphate buffer, pH 7.4, containing 1 mg/mL of bovine serum albumin

707525

3.1.1.6

1.54

-

-

23597

3.1.1.6

2.63

-

pH 7.8, 45°C

653087

3.1.1.6

2.7

-

-

23600

3.1.1.6

7.8

-

pH 6.5

701417

3.1.1.72

0.056

-

pH 6.5, 37°C, acetylxylan esterase Axe6B

664492

3.1.1.72

0.084

-

pH 6.5, 37°C, acetylxylan esterase Axe6A

664492

3.1.1.72

1.54

-

-

23597

3.1.1.72

2.66

-

-

23600

3.1.1.73

0.01

-

in 20% N,N-dimethyl formamide, 50 mM acetate buffer, pH 5, with 0.05 ml enzyme solution, at 37°C for 10 min

699282

3.1.1.73

0.25

-

pH 6.0, 55°C

737582, 741805

3.1.1.73

0.5

-

20°C, pH 7.4

679997

3.1.1.73

10

-

-

208310

3.1.1.79

0.54

-

Vmax: 0.019 mM/min

706584

3.1.1.79

0.54

-

Vmax: 0.019 mM/min

706584

3.1.2.12

0.54

-

pH 8.0, 37°C, recombinant YeiG mutant D255A

665750

3.1.2.12

0.57

-

recombinant enzyme, pH 7.2, 37°C

649455

3.1.2.12

0.8

-

pH 8.0, 37°C, recombinant YeiG mutant D80A

665750

3.1.2.12

1.01

-

pH 8.0, 37°C, recombinant YeiG mutant D199A

665750

3.1.2.12

1.03

-

pH 8.0, 37°C, recombinant wild-type YeiG

665750

3.1.2.12

1.06

-

pH 8.0, 37°C, recombinant YeiG mutant C26A

665750

3.1.2.12

1.28

-

pH 8.0, 37°C, recombinant YeiG mutant C54A

665750

3.1.2.12

1.3

-

pH 8.0, 37°C, recombinant YeiG mutant D218A

665750

3.1.1.55

2 entries

3.1.1.56

3 entries

3.1.1.59

2 entries

3.1.1.6

4 entries

3.1.1.72

4 entries

3.1.1.73

4 entries

3.1.1.79

2 entries

3.1.2.12

8 entries

References & Links

Literature References (104)

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Show Reference (104 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

23487

3654630

Characterization of affinity-purified juvenile hormone esterase from Trichoplusia ni

1987

Hanzlik, T.N.; Hammock, B.D.

J. Biol. Chem.

28

13584-13591

23591

-

Purification and properties of two acetylxylan esterases of Trichoderma reesei

1991

Sundberg, M.; Poutanen, K.

Biotechnol. Appl. Biochem.

13

1-11

23594

8756392

Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum

1996

Egana, L.; Gutierrez, R.; Caputo, V.; Peirano, A.; Steiner, J.; Eyzaguirre, J.

Biotechnol. Appl. Biochem.

24

33-39

23597

10215579

Purification and characterization of an acetyl xylan esterase from Bacillus pumilus

1998

Degrassi, G.; Okeke, B.C.; Bruschi, C.V.; Venturi, V.

Appl. Environ. Microbiol.

64

789-792

23600

2082827

Purification and properties of an acetylxylan esterase from Fibrobacter succinogenes S85

1990

McDermid, K.P.; Forsberg, C.W.; MacKenzie, C.R.

Appl. Environ. Microbiol.

56

3805-3810

35195

-

Purification and some properties of an esterase from yeast

1986

Toshimitsu, N.; Hamada, H.; Kojima, M.

J. Ferment. Technol.

64

459-462

35199

6870256

Acylhydrolases from parsley (Petroselinum hortense). Relative distribution and properties of four esterases hydrolyzing malonic acid hemiesters of flavonoid glucosides

1983

Matern, U.

Arch. Biochem. Biophys.

224

261-271

35203

4214592

Characterization of the esterases of feline serum

1974

Ecobichon, D.J.

Can. J. Biochem.

52

1073-1078

35223

-

An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans

1988

Poutanen, K.; Sundberg, M.

Appl. Microbiol. Biotechnol.

28

419-424

35226

3001718

Kinetic properties of a sex pheromone-degrading enzyme: the sensillar esterase of Antheraea polyphemus

1985

Vogt, R.G.; Riddiford, L.M.; Prestwich, G.D.

Proc. Natl. Acad. Sci. USA

82

8827-8831

35230

7445676

Isolierung und Charakterisierung einer Acetylester-Hydrolase aus Aspergillus niger

1980

Schoebel, B.; Pollmann, W.

Z. Naturforsch. C

35

696-698

35236

-

Purification and properties of an acetyl ester hydrolase (acetylesterase) from Lactobacillus plantarum

1972

Oterholm, A.; Witter, L.D.; Ordal, Z.J.

J. Dairy Sci.

55

8-13

35241

7576539

An acetylglucomannan esterase of Aspergillus oryzae; purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan

1995

Tenkanen, M.; Thornton, J.; Viikari, L.

J. Biotechnol.

42

197-206

80990

10427036

Purification and properties of an esterase from the yeast Saccharomyces cerevisiae and identification of the encoding gene

1999

Degrassi, G.; Uotila, L.; Klima, R.; Venturi, V.

Appl. Environ. Microbiol.

65

3470-3472

94408

3149520

Sialate O-acetylesterases: key enzymes in sialic acid catabolism

1988

Schauer, R.; Reuter, G.; Stoll, S.

Biochimie

70

1511-1519

94410

3242542

Isolation and characterization of sialate 9(4)-O-acetylesterase from influenza C virus

1988

Schauer, R.; Reuter, G.; Stoll, S.; Posadas del Rio, F.; Herrler, G.; Klenk, H.D.

Biol. Chem. Hoppe-Seyler

369

1121-1130

94417

2808434

O-Acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids

1989

Higa, H.H.; Manzi, A.; Varki, A.

J. Biol. Chem.

264

19435-19442

94419

2695768

Sialate 9-O-acetylesterase from rat liver

1989

Higa, H.H.; Manzi, A.; Diaz, S.; Varki, A.

Methods Enzymol.

179

409-415

114133

5073758

Human erythrocyte acetylcholinesterase; purification, properties and kinetic behavior

1972

Ciliv, G.; Oezand, P.T.

Biochim. Biophys. Acta

284

136-156

170667

237223

Cephalosporin acetylesterase (Bacillus subtilis)

1978

Abbott, B.J.; Fukuda, D.S.

Methods Enzymol.

43

731-734

170979

2246262

Human monocyte carboxylesterase. Purification and kinetics

1990

Saboori, A.M.; Newcombe, D.S.

J. Biol. Chem.

265

19792-19799

170981

-

Purification, characterization and properties of carboxylesterase from the midgut of the silkworm, Bombyx mori L

1996

Siddalinga Murthy, K.R.; Veerabhadrappa, P.S.

Insect Biochem. Mol. Biol.

26

287-296

170987

6380369

Purification and properties of carboxylesterase B of Escherichia coli

1984

Goullet, P.; Picard, B.; Laget, P.F.

Ann. Microbiol.

135A

375-387

171004

603629

The properties of a carboxylesterase from the peach-potato aphid, Myzus persicae (Sulz.), and its role in conferring insecticide resistance

1977

Devonshire, A.L.

Biochem. J.

167

675-683

171017

3651439

Purification and characterization of a carboxylesterase from the intestine of the nematode Caenorhabditis elegans

1987

McGhee, J.D.

Biochemistry

26

4101-4107

171026

7764506

Cloning of Pseudomonas fluorescens carboxylesterase gene and characterization of its product expressed in Escherichia coli

1994

Kim, Y.S.; Lee, H.B.; Choi, K.D.; Park, S.; Yoo, O.J.

Biosci. Biotechnol. Biochem.

58

111-116

208302

-

Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum

1992

Castanares, A.; McCrae, S.I.; Wood, T.M.

Enzyme Microb. Technol.

14

875-884

208310

9836439

Purification and characterization of a feruloylesterase from Aspergillus awamori

1998

Koseki, T.; Furuse, S.; Iwano, K.; Matsuzawa, H.

Biosci. Biotechnol. Biochem.

62

2032-2034

208312

10231593

Feruloyl esterase from Aspergillus sp.: Purification, properties, and action on natural substrates

1999

Dzedzyulya, E.I.; Becker, E.G.; Okunev, O.N.; Sinitsyn, A.P.

Biochemistry (Moscow)

64

405-410

208316

11082184

A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module

2000

Kroon, P.A.; Williamson, G.; Fish, N.M.; Archer, D.B.; Belshaw, N.J.

Eur. J. Biochem.

267

6740-6752

646021

2383281

Aspirin hydrolyzing esterases from rat liver cytosol

1990

Kim, D.H.; Yang, Y.S.; Jakoby, W.B.

Biochem. Pharmacol.

40

481-487

646032

4076172

Purification and characterization of esterases D1 and D2 from human erythrocytes. Evidence that they are monomers

1985

Matsuo, K.; Kobayashi, K.; Hagiwara, K.; Kajii, T.

Eur. J. Biochem.

153

217-222

646036

-

Esterase D polymorphism and partial characterization of red blood cell esterases in cattle and buffalo populations

1996

Lama, S.N.D.; Lama, M.A.D.; Mestriner, M.A.; Mortari, N.

Braz. J. Genet.

19

243-248

646527

8565784

Comparison of purified human and rabbit serum paraoxonases

1995

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Cloning and characterization of EstC from Burkholderia gladioli, a novel-type esterase related to plant enzymes

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Purification and characterization of trans-permethrin metabolizing microsomal esterases from workers of the eastern subterranean termite, Reticulitermes flavipes (Kollar)

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Biochemical characterization of esterases active in hydrolysing xenobiotics in wheat and competing weeds

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Isolation, characterization, and heterologous expression of a carboxylesterase of Pseudomonas aeruginosa PAO1

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The effect of piperonyl butoxide on pyrethroid-resistance-associated esterases in Helicoverpa armigera (Huebner) (Lepidoptera: Noctuidae)

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Partial purification and characterization of a methyl-parathion resistance-associated general esterase in Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae)

2004

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Biochemical and genetic polymorphisms for carboxylesterase and acetylesterase in grape clones of Vitis vinifera L. (Vitaceae) cultivars

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The psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125 possesses a gene coding for a cold-adapted feruloyl esterase activity that shares homology with esterase enzymes from gamma-proteobacteria and yeast

2007

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Purification and partial characterization of acetic acid esterase from malted finger millet (Eleusine coracana, Indaf-15)

2007

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An eleven amino acid residue deletion expands the substrate specificity of acetyl xylan esterase II (AXE II) from Penicillium purpurogenum

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Expression and characterization of a new esterase cloned directly from Agrobacterium tumefaciens genome

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In vitro acetylcholinesterase inhibitory properties of thymol, carvacrol and their derivatives thymoquinone and thymohydroquinone

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Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans

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B-type esterases in the snail Xeropicta derbentina: an enzymological analysis to evaluate their use as biomarkers of pesticide exposure

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Organophosphates resistance in the B-biotype of Bemisia tabaci (Hemiptera: Aleyrodidae) is associated with a point mutation in an ace1-type acetylcholinesterase and overexpression of carboxylesterase

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Differential mRNA expression levels and gene sequences of carboxylesterase in both deltamethrin resistant and susceptible strains of the cotton aphid, Aphis gossypii

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A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression

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Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition

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Selective inhibition of butyrylcholinesterase in vivo in horses by the feed-through larvacide Equitrol

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Purification and characterization of the enantioselective esterase from Kluyveromyces marxianus CBS 1553

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Characterization of a novel oligomeric SGNH-arylesterase from Sinorhizobium meliloti 1021

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Purification and characterization of a novel extracellular carboxylesterase from the moderately halophilic bacterium Thalassobacillus sp. strain DF-E4

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Molecular cloning and characterization of a novel SGNH arylesterase from the goat rumen contents

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Purification and characterisation of a carboxylesterase from a chlorpyrifos-methyl-resistant strain of Oryzaephilus surinamensis (Coleoptera: Silvanidae)

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Purification and characterization of an intracellular lipase from pleopods of whiteleg shrimp (Litopenaeus vannamei)

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Heterologous expression and characterization of the carboxylesterase from Geobacillus stearothermophilus

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Structural characterization and function determination of a nonspecific carboxylate esterase from the amidohydrolase superfamily with a promiscuous ability to hydrolyze methylphosphonate esters

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Biochemistry

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Expression and characterization of a thermostable acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis involved in the degradation of insoluble cellulose acetate

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Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima

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Acidic-alkaline ferulic acid esterase from Chaetomium thermophilum var. dissitum: Molecular cloning and characterization of recombinant enzyme expressed in Pichia pastoris

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Crystal structure of Thermotoga maritima acetyl esterase complex with a substrate analog Insights into the distinctive substrate specificity in the CE7 carbohydrate esterase family

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Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7

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Singh, M.; Manoj, N.

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2017

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1-Naphthyl acetate a chromogenic substrate for the detection of erythrocyte acetylcholinesterase activity

2018

Chowdhary, S.; Bhattacharyya, R.; Banerjee, D.

Biochimie

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Characterization of cross-linked immobilized arylesterase from Gluconobacter oxydans 621H with activity toward cephalosporin C and 7-aminocephalosporanic acid

2016

Inmaculada, N.; Francisco, G.

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Characterization and kinetics of juvenile hormone esterase from Spodoptera littoralis (Boisd.) and S. frugiperda (J. E. Smith) (Lepidoptera Noctuidae)

2015

El-Sheikh, E.

Egypt. J. Biol. Pest Control

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Structural and biochemical characterization of an octameric carbohydrate acetylesterase from Sinorhizobium meliloti

2016

Oh, C.; Ryu, B.H.; An, D.R.; Nguyen, D.D.; Yoo, W.; Kim, T.; Ngo, T.D.; Kim, H.S.; Kim, K.K.; Kim, T.D.

FEBS Lett.

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Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase

2016

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Parasitology

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Cloning, purification and characterization of acetyl xylane esterase from Anoxybacillus flavithermus DSM 2641(T) with activity on low molecular-weight acetates

2015

Eminoglu, A.; Uelker, S.; Sandalli, C.

Protein J.

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Decreasing the level of ethyl acetate in ethanolic fermentation broths of Escherichia coli KO11 by expression of Pseudomonas putida estZ esterase

2002

Hasona, A.; York, S.; Yomano, L.; Ingram, L.; Shanmugam, K.

Appl. Environ. Microbiol.

68

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Links to other databases for Alpha-naphthyl acetate

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