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Ligand p-nitrophenyl-alpha-L-arabinofuranoside

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

665997, 663572

1qw9, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

665997, 663572

6sxr, 3D-view

3.2.1.55

2 entries

Substrate in Enzyme-catalyzed Reactions (32 results)

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Show Substrate (32 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.73

4-nitrophenyl alpha-L-arabinofuranoside + H2O = alpha-L-arabinofuranose + 4-nitrophenol

710685

-

3.1.1.73

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

208305

-

3.1.1.73

2 entries

3.2.1.126

p-nitrophenyl alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

650284

-

3.2.1.193

4-nitrophenyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinofuranose

752455

-

3.2.1.21

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

326317, 742537, 739692, 326292

-

3.2.1.37

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

750780, 683715, 707206, 707563, 744199, 679713, 664078, 707536, 683091, 664409, 666625, 744108, 750026, 715881, 749706, 739579, 708923, 667008, 749718, 750334, 707191, 707192, 715674, 749634, 751314

-

3.2.1.37

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinofuranose

749653, 745562

-

3.2.1.37

p-nitrophenyl alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

136275, 136283, 136279, 136295

-

3.2.1.37

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

655008

-

3.2.1.37

4 entries

3.2.1.40

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

654992

-

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

288830, 654847, 288820, 656328, 288822, 714042, 654276, 716193, 714571, 655653, 655156, 655175, 710292, 715550, 664528, 654273, 696279, 656094, 710309, 715881, 715805, 713698, 713903, 737424, 743945, 737390, 744427, 744129, 744111, 747342, 750429, 750122, 656191, 749551, 744069, 715952, 715318, 657222, 715780

1qw9, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

288830, 654847, 288820, 656328, 288822, 714042, 654276, 716193, 714571, 655653, 655156, 655175, 710292, 715550, 664528, 654273, 696279, 656094, 710309, 715881, 715805, 713698, 713903, 737424, 743945, 737390, 744427, 744129, 744111, 747342, 750429, 750122, 656191, 749551, 744069, 715952, 715318, 657222, 715780

6sxr, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinofuranose

738310, 707245, 707261, 737510, 713826, 732171, 732166, 732326, 732329, 731195, 732579, 737892, 732745, 732843, 731162, 731198, 731730, 737905, 737909, 742926, 752571, 755100, 710186, 732276, 677743, 731785, 745562

1qw9, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinofuranose

738310, 707245, 707261, 737510, 713826, 732171, 732166, 732326, 732329, 731195, 732579, 737892, 732745, 732843, 731162, 731198, 731730, 737905, 737909, 742926, 752571, 755100, 710186, 732276, 677743, 731785, 745562

6sxr, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinose

696279, 737311, 738475, 737855

1qw9, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinose

696279, 737311, 738475, 737855

6sxr, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = ?

715312

1qw9, 3D-view

3.2.1.55

4-nitrophenyl alpha-L-arabinofuranoside + H2O = ?

715312

6sxr, 3D-view

3.2.1.55

p-nitrophenyl alpha-L-arabinofuranoside + benzyl-alpha-D-xylopyranoside = ?

664519

1qw9, 3D-view

3.2.1.55

p-nitrophenyl alpha-L-arabinofuranoside + benzyl-alpha-D-xylopyranoside = ?

664519

6sxr, 3D-view

3.2.1.55

p-nitrophenyl alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinofuranose

677785, 695802

1qw9, 3D-view

3.2.1.55

p-nitrophenyl alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinofuranose

677785, 695802

6sxr, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

665997, 664420, 663978, 663572, 666636, 664407, 700791

1qw9, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + alpha-L-arabinofuranose

665997, 664420, 663978, 663572, 666636, 664407, 700791

6sxr, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinofuranose

681118, 678454, 679713, 680411, 678383, 678050, 678677, 677763, 677783, 679963, 677758, 696798, 700043, 700334, 700791, 677743

1qw9, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinofuranose

681118, 678454, 679713, 680411, 678383, 678050, 678677, 677763, 677783, 679963, 677758, 696798, 700043, 700334, 700791, 677743

6sxr, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinose

288812, 288813, 288816, 288822, 288823, 288828, 288829, 288835, 288840, 288842, 288845, 288846, 288850, 288824, 288834, 288843, 288847, 171754, 171764, 288811, 288815, 288818, 288826, 288830, 288833, 288838, 288841, 288849, 288844, 288827, 288837, 288839, 288819, 288848, 288817, 695816

1qw9, 3D-view

3.2.1.55

p-nitrophenyl-alpha-L-arabinofuranoside + H2O = p-nitrophenol + L-arabinose

288812, 288813, 288816, 288822, 288823, 288828, 288829, 288835, 288840, 288842, 288845, 288846, 288850, 288824, 288834, 288843, 288847, 171754, 171764, 288811, 288815, 288818, 288826, 288830, 288833, 288838, 288841, 288849, 288844, 288827, 288837, 288839, 288819, 288848, 288817, 695816

6sxr, 3D-view

3.2.1.55

18 entries

3.2.1.58

4-nitrophenyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinofuranose

738437

-

3.2.1.8

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

656559, 750432, 750497

-

3.2.1.99

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + alpha-L-arabinofuranose

750239

-

3.2.1.B28

4-nitrophenyl alpha-L-arabinofuranoside + H2O = 4-nitrophenol + L-arabinose

735531

-

Product in Enzyme-catalyzed Reactions (15 results)

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Show Product (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.6

4-nitrophenyl-2-O-acetyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + acetate

-

-

3.1.1.6

4-nitrophenyl-5-O-acetyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + acetate

-

-

3.1.1.73

4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O = ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside

-

-

3.1.1.73

4-nitrophenyl 3-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl alpha-L-arabinofuranoside + ferulate

-

-

3.1.1.73

4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl alpha-L-arabinofuranoside + ferulate

-

-

3.1.1.73

4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O = ferulic acid + 4-nitrophenyl alpha-L-arabinofuranoside

-

-

3.1.1.73

4-nitrophenyl 2-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + ferulate

-

-

3.1.1.73

4-nitrophenyl 2-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + trans-ferulate

-

-

3.1.1.73

4-nitrophenyl 2-O-acetyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + acetate

-

-

3.1.1.73

4-nitrophenyl 2-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O = ferulic acid + 4-nitrophenyl-alpha-L-arabinofuranoside

-

-

3.1.1.73

4-nitrophenyl 3-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + ferulate

-

-

3.1.1.73

4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + ferulate

-

-

3.1.1.73

4-nitrophenyl 5-O-(E)-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + trans-ferulate

-

-

3.1.1.73

4-nitrophenyl 5-O-acetyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + acetate

-

-

3.1.1.73

4-nitrophenyl 5-O-trans-feruloyl-alpha-L-arabinofuranoside + H2O = 4-nitrophenyl-alpha-L-arabinofuranoside + trans-ferulate

-

-

3.1.1.6

2 entries

3.1.1.73

13 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.37

substrate inhibition if concentration higher than 12 mM

136283

-

3.2.1.55

-

715805

1qw9, 3D-view

3.2.1.55

-

715805

6sxr, 3D-view

3.2.1.55

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (10 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (10 entries)

EC NUMBER

ENZYME 3D STRUCTURE

3.2.1.55

1qw9, 3D-view

3.2.1.55

6sxr, 3D-view

3.2.1.55

1qw9, 3D-view

3.2.1.55

6sxr, 3D-view

3.2.1.55

1qw9, 3D-view

3.2.1.55

6sxr, 3D-view

3.2.1.55

1qw9, 3D-view

3.2.1.55

6sxr, 3D-view

3.2.1.55

1qw9, 3D-view

3.2.1.55

6sxr, 3D-view

3.2.1.55

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (107 results)

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Show Turnover Number (107 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.2.1.126

118

-

pH 6.5, 30°C

650284

3.2.1.37

0.0000036

-

mutant E186A, pH 7.0, 25°C

707206

3.2.1.37

0.0000044

-

mutant E186A, pH 8.0, 25°C

707206

3.2.1.37

0.0000045

-

mutant E186A, pH 6.0, 25°C

707206

3.2.1.37

1.18

-

pH 6.2, 40°C

707191

3.2.1.37

2.81

-

pH 5.0, 40°C

750334

3.2.1.37

3.05

-

wild-type, pH 8.0, 25°C

707206

3.2.1.37

3.13

-

wild-type, pH 6.0, 25°C

707206

3.2.1.37

3.14

-

pH 7.0, 25°C

707563

3.2.1.37

3.28

-

wild-type, pH 7.0, 25°C

707206

3.2.1.37

3.34

-

presence of tris(hydroxymethyl)aminomethane, pH 7.0, 25°C

707563

3.2.1.37

4.7

-

37°C

683715

3.2.1.37

31.5

-

pH 4.5, 37°C

683091

3.2.1.37

113

-

pH 4.0, 40°C

739579

3.2.1.37

143

-

at pH 3.0 and 50°C

749653

3.2.1.37

2201.64

-

pH 6.0, 90°C

750026

3.2.1.55

0.0000134

-

pH 5.3, 25°C, mutant enzyme D127A

678454

3.2.1.55

0.000239

-

pH 5.3, 25°C, mutant enzyme E186A

678454

3.2.1.55

0.0005

-

pH 4.1, 25°C, mutant enzyme E223Q

678050

3.2.1.55

0.000936

-

pH 5.3, 25°C, mutant enzyme D14A

678454

3.2.1.55

0.002

-

mutant enzyme D20N, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.003

-

pH 4.1, 25°C, mutant enzyme D221N

678050

3.2.1.55

0.00553

-

pH 5.3, 25°C, mutant enzyme R290G

678454

3.2.1.55

0.014

-

pH 6.5, mutant enzyme D299G

678050

3.2.1.55

0.0149

-

pH 5.3, 25°C, mutant enzyme R290A

678454

3.2.1.55

0.016

-

pH 4.1, 25°C, mutant enzyme D299N

678050

3.2.1.55

0.0175

-

pH 5.3, 25°C, mutant enzyme R290V

678454

3.2.1.55

0.02

-

ph 5.5, 37°C, recombinant wild-type enzyme

732171

3.2.1.55

0.039

-

pH 5.0, 37°C

732166

3.2.1.55

0.0694

-

pH 4.0, 37°C, mutant enzyme N83Q/N202Q

678383

3.2.1.55

0.0755

-

pH 4.0, 37°C, mutant enzyme N202Q

678383

3.2.1.55

0.08

-

pH 6.0, 40°C, mutant E175A

656094

3.2.1.55

0.08

-

pH 4.1, 25°C, mutant enzyme D299G

678050

3.2.1.55

0.0898

-

pH 4.0, 37°C, mutant enzyme N83Q

678383

3.2.1.55

0.099

-

pH 4.0, 37°C, wild-type enzyme

678383

3.2.1.55

0.11

-

wild type enzyme, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.158

-

pH 5.3, 25°C, mutant enzyme R290H

678454

3.2.1.55

0.27

-

at pH 4.5 and 35°C

749551

3.2.1.55

0.275

-

pH 5.3, 25°C, mutant enzyme R290Q

678454

3.2.1.55

0.3

-

pH 4.1, 25°C, mutant enzyme E310G

678050

3.2.1.55

0.38

-

pH 5.0, 37°C

732166

3.2.1.55

0.39

-

pH 5.8, 60°C, mutant E176A

657222

3.2.1.55

0.426

-

pH 5.3, 25°C, mutant enzyme R290K

678454

3.2.1.55

0.53

-

pH 5.8, 60°C, mutant E298D

657222

3.2.1.55

0.54

-

mutant R69H/G179F/L352M, pH 7.0, 45°C

737311

3.2.1.55

0.56

-

mutant enzyme N159A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.58

-

mutant R69H/N216W/L352M, pH 7.0, 45°C

737311

3.2.1.55

0.62

-

mutant enzyme L289A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.63

-

pH 5.8, 60°C, mutant E28A

657222

3.2.1.55

0.65

-

pH 5.8, 60°C, mutant E176D

657222

3.2.1.55

0.68

-

pH 4.1, 25°C, mutant enzyme D170N

678050

3.2.1.55

0.97

-

mutant R69H/L352M, pH 7.0, 45°C

737311

3.2.1.55

1.04

-

pH 5.8, 60°C, mutant E298Q

657222

3.2.1.55

1.07

-

mutant enzyme Y192A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

1.08

-

pH 5.8, 60°C, mutant E28D

657222

3.2.1.55

1.09

-

pH 5.3, 25°C, mutant enzyme F508A

678454

3.2.1.55

1.36

-

37°C

681118

3.2.1.55

2.1

-

pH 4.6, 37°C

738310

3.2.1.55

2.29

-

mutant R69H, pH 7.0, 45°C

737311

3.2.1.55

2.45

-

-

700334

3.2.1.55

2.68

-

pH 5.3, 25°C, wild-type enzyme

678454

3.2.1.55

2.73

-

in 50 mM sodium citrate buffer (pH 4.0), at 30°C

713826

3.2.1.55

2.84

-

pH 6.5, wild-type enzyme

678050

3.2.1.55

4.55

-

mutant enzyme N159L, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

4.72

-

pH 5.7, 50°C, recombinant full-length enzyme

732745

3.2.1.55

4.78

-

pH 5.7, 50°C, recombinant catalytic module CtGH43

732745

3.2.1.55

5.6

-

in 50 mM phosphate/citrate buffer pH 7.0, at 40°C

715805

3.2.1.55

5.95

-

pH 5.8, 60°C, mutant E28Q

657222

3.2.1.55

9.33

-

pH 5.3, 25°C, mutant enzyme F31A

678454

3.2.1.55

14.3

-

in 50 mM potassium phosphate buffer (pH 7.0), at 50°C

715952

3.2.1.55

14.3

-

enzyme AFQ1, pH 5.0, 37°C

654847

3.2.1.55

21

-

pH 4.1, 25°C, wild-type enzyme

678050

3.2.1.55

22

-

pH 4.1, 25°C, mutant enzyme E223G

678050

3.2.1.55

23

-

pH 6.0, 60°C

737905

3.2.1.55

24

-

Tx-Abf-C180A mutant, 60°C

696279

3.2.1.55

35

-

Tx-Abf-M94_I103delinsGG mutant, 60°C

696279

3.2.1.55

36.7

-

pH 5.8, 60°C, mutant E176Q

657222

3.2.1.55

43

-

mutant S160G, pH 5.0, 40°C

737892

3.2.1.55

50

-

wild-type, pH 5.0, 40°C

737892

3.2.1.55

50.17

-

recombinant enzyme, pH 5.0, 40°C

731195

3.2.1.55

59.3

-

enzyme AFS1, pH 5.0, 37°C

654847

3.2.1.55

62.9

-

isoform Abf51B, at pH 7.0 and 40°C

744129

3.2.1.55

77

-

mutant W99F, pH 5.8, 60°C

731785

3.2.1.55

87

-

pH 6.0, 40°C, wild-type enzyme

656094

3.2.1.55

97

-

mutant H98F/W99F, pH 5.8, 60°C

731785

3.2.1.55

103

-

pH 7.0, 37°C

663978

3.2.1.55

137

-

mutant W99A, pH 5.8, 60°C

731785

3.2.1.55

139

-

wild-type, pH 7.0, 45°C

737311

3.2.1.55

149.8

-

isoform Abf51A, at pH 7.0 and 40°C

744129

3.2.1.55

151

-

pH 5.0, 95°C

738475

3.2.1.55

154

-

mutant H98A/W99A, pH 5.8, 60°C

731785

3.2.1.55

165

-

Tx-Abf-W99A mutant, 60°C

696279

3.2.1.55

192

-

mutant H98A, pH 5.8, 60°C

731785

3.2.1.55

199

-

mutant H98F, pH 5.8, 60°C

731785

3.2.1.55

226

-

in 50 mM citric acid buffer (pH 5.5), at 80°C

715312

3.2.1.55

233

-

mutant L352M, pH 7.0, 45°C

737311

3.2.1.55

285

-

in 50 mM citric acid buffer (pH 5.5), at 80°C

715312

3.2.1.55

295

-

-

700043

3.2.1.55

306

-

-

700043

3.2.1.55

328

-

pH 6.5, 60°C

737909

3.2.1.55

355

-

Tx-Abf, 60°C

696279

3.2.1.55

575

-

wild-type enzyme, pH 5.8, 60°C

731785

3.2.1.55

3900

-

at pH 6.0 and 80°C

744111

3.2.1.55

4100

-

pH 5.8, 60°C, wild-type enzyme

657222

3.2.1.37

15 entries

3.2.1.55

88 entries

3.2.1.58

123.6

-

pH 6.0, 40°C

738437

3.2.1.8

85.5

-

pH 5.0, 50°C

656559

3.2.1.8

104

-

at pH 5.0 and 50°C

750432

3.2.1.8

2 entries

K_M Value (163 results)

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Show KM Value (163 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.126

0.27

-

pH 6.5, 30°C

650284

3.2.1.21

0.017

-

-

326317

3.2.1.37

0.133

-

mutant E186A, pH 8.0, 25°C

707206

3.2.1.37

0.152

-

mutant E186A, pH 7.0, 25°C

707206

3.2.1.37

0.177

-

mutant E186A, pH 6.0, 25°C

707206

3.2.1.37

0.497

-

pH 6.2, 40°C

707191

3.2.1.37

0.715

-

wild-type, pH 6.0, 25°C

707206

3.2.1.37

0.94

-

37°C

683715

3.2.1.37

1.08

-

wild-type, pH 7.0, 25°C

707206

3.2.1.37

1.31

-

pH 5.0, 40°C

750334

3.2.1.37

4.09

-

wild-type, pH 8.0, 25°C

707206

3.2.1.37

4.54

-

pH 4.0, 40°C

739579

3.2.1.37

4.6

-

-

136283

3.2.1.37

5.8

-

at pH 3.0 and 50°C

749653

3.2.1.37

6.165

-

pH 6.0, 90°C

750026

3.2.1.37

6.8

-

pH 4.5, 37°C

683091

3.2.1.55

0.001

-

mutant enzyme D20N, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.04

-

pH 5.7, 50°C, recombinant catalytic module CtGH43

732745

3.2.1.55

0.042

-

mutant E194A

288848

3.2.1.55

0.05

-

pH 5.7, 50°C, recombinant full-length enzyme

732745

3.2.1.55

0.05

-

pH 4.1, 25°C, mutant enzyme D299N

678050

3.2.1.55

0.08

-

-

288822

3.2.1.55

0.082

-

-

288812, 288816

3.2.1.55

0.09

-

mutant R69H, pH 7.0, 45°C

737311

3.2.1.55

0.098

-

-

700334

3.2.1.55

0.1

-

isoform Abf51B, at pH 7.0 and 40°C

744129

3.2.1.55

0.139

-

-

695816

3.2.1.55

0.14

-

pH 6.0, 40°C, mutant E175A

656094

3.2.1.55

0.15

-

-

663572

3.2.1.55

0.17

-

-

677763

3.2.1.55

0.18

-

pH 9.0

655653

3.2.1.55

0.18

-

-

288848

3.2.1.55

0.186

-

pH 5.0, 95°C

738475

3.2.1.55

0.21

-

in 50 mM sodium acetate buffer (pH 5.5), at 37°C

715318

3.2.1.55

0.21

-

pH 4.1, 25°C, mutant enzyme D299G

678050

3.2.1.55

0.21

-

pH 6.5, mutant enzyme D299G

678050

3.2.1.55

0.22

-

pH 7.0, 37°C

654276

3.2.1.55

0.22

-

-

288824

3.2.1.55

0.22

-

pH 4.1, 25°C, mutant enzyme D221N

678050

3.2.1.55

0.23

-

pH 6.0

696798

3.2.1.55

0.25

-

wild-type, pH 7.0, 45°C

737311

3.2.1.55

0.25

-

-

663978

3.2.1.55

0.26

-

37°C

681118

3.2.1.55

0.28

-

pH 6.0, 45°C, isozyme ABF2

655156

3.2.1.55

0.295

-

pH 6.0, 45°C

654273

3.2.1.55

0.3

-

pH 5.8, 60°C, mutant E176D

657222

3.2.1.55

0.3

-

pH 4.1, 25°C, mutant enzyme D170N

678050

3.2.1.55

0.31

-

pH 6.5, 60°C

737909

3.2.1.55

0.31

-

isoenzyme ABF3

288837

3.2.1.55

0.31

-

pH 6.5, wild-type enzyme

678050

3.2.1.55

0.32

-

pH 4.1, 25°C, wild-type enzyme

678050

3.2.1.55

0.35

-

isoenzyme ABF1

288837

3.2.1.55

0.37

-

pH 4.1, 25°C, mutant enzyme E223G

678050

3.2.1.55

0.39

-

pH 6.0, 45°C, isozyme ABF1

655156

3.2.1.55

0.41

-

pH 5.8, 60°C, mutant E176Q

657222

3.2.1.55

0.42

-

-

288832, 700043

3.2.1.55

0.43

-

pH 5.8, 60°C, mutant E176A

657222

3.2.1.55

0.46

-

pH 6.0, 60°C

737905

3.2.1.55

0.47

-

isoenzyme ABF2

288837

3.2.1.55

0.48

-

mutant R69H/N216W/L352M, pH 7.0, 45°C

737311

3.2.1.55

0.48

-

-

288830

3.2.1.55

0.48

-

strain B

288841

3.2.1.55

0.49

-

-

700043

3.2.1.55

0.5

-

wild type enzyme, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

0.5

-

-

288844, 288829

3.2.1.55

0.51

-

pH 5.8, 60°C, mutant E28D

657222

3.2.1.55

0.52

-

alpha-L-arabinofuranosidase B

171764

3.2.1.55

0.53

-

-

288820

3.2.1.55

0.6

-

at pH 6.0 and 80°C

744111

3.2.1.55

0.6

-

-

288830, 288828, 664407

3.2.1.55

0.64

-

wild-type, pH 5.0, 40°C

737892

3.2.1.55

0.64

-

recombinant enzyme, pH 5.0, 40°C

731195

3.2.1.55

0.65

-

in 50 mM sodium citrate buffer (pH 4.0), at 30°C

713826

3.2.1.55

0.65

-

pH 6.0, 40°C, wild-type enzyme

656094

3.2.1.55

0.66

-

-

288822

3.2.1.55

0.68

-

alpha-L-arabinofuranosidase A

171764

3.2.1.55

0.69

-

mutant R69H/G179F/L352M, pH 7.0, 45°C

737311

3.2.1.55

0.69

-

pH 4.0, 37°C, mutant enzyme N83Q/N202Q

678383

3.2.1.55

0.7

-

-

288822

3.2.1.55

0.7

-

isoform Abf51A, at pH 7.0 and 40°C

744129

3.2.1.55

0.7

-

pH 5.8, 60°C, wild-type enzyme

657222

3.2.1.55

0.7

-

-

678677

3.2.1.55

0.72

-

wild-type enzyme, pH 5.8, 60°C

731785

3.2.1.55

0.77

-

in 50 mM potassium phosphate buffer (pH 7.0), at 50°C

715952

3.2.1.55

0.77

-

-

288846

3.2.1.55

0.771

-

pH 5.3, 25°C, mutant enzyme D14A

678454

3.2.1.55

0.779

-

pH 5.3, 25°C, mutant enzyme D127A

678454

3.2.1.55

0.8

-

-

288822

3.2.1.55

0.81

-

pH 5.3, 25°C, wild-type enzyme

678454

3.2.1.55

0.82

-

-

288817

3.2.1.55

0.86

-

enzyme AFQ1, pH 5.0, 37°C

654847

3.2.1.55

0.86

-

pH 4.0, 37°C, mutant enzyme N202Q

678383

3.2.1.55

0.87

-

mutant H98F, pH 5.8, 60°C

731785

3.2.1.55

0.88

-

pH 4.1, 25°C, mutant enzyme E223Q

678050

3.2.1.55

0.89

-

mutant S160G, pH 5.0, 40°C

737892

3.2.1.55

0.9

-

isoenzyme AF53

288839

3.2.1.55

0.91

-

pH 5.8, 60°C, mutant E298Q

657222

3.2.1.55

0.93

-

in 50 mM acetate buffer, pH 5.0, at 50°C

713698

3.2.1.55

1.04

-

pH 5.8, 60°C, mutant E28A

657222

3.2.1.55

1.04

-

pH 4.0, 37°C, wild-type enzyme

678383

3.2.1.55

1.05

-

-

677785

3.2.1.55

1.07

-

pH 4.0, 37°C, mutant enzyme N83Q

678383

3.2.1.55

1.1

-

in 50 mM citric acid buffer (pH 5.5), at 80°C

715312

3.2.1.55

1.1

-

mutant enzyme N159L, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

1.1

-

isoenzyme AF35

288839

3.2.1.55

1.11

-

pH 5.8, 60°C, mutant E298D

657222

3.2.1.55

1.2

-

-

288830, 288841

3.2.1.55

1.2

-

alpha-L-arafase I

288827

3.2.1.55

1.23

-

mutant R69H/L352M, pH 7.0, 45°C

737311

3.2.1.55

1.23

-

-

288841

3.2.1.55

1.29

-

in 50 mM citric acid buffer (pH 5.5), at 80°C

715312

3.2.1.55

1.3

-

-

288813, 288822

3.2.1.55

1.32

-

enzyme AFS1, pH 5.0, 37°C

654847

3.2.1.55

1.33

-

pH 5.3, 25°C, mutant enzyme E186A

678454

3.2.1.55

1.36

-

at pH 4.5 and 35°C

749551

3.2.1.55

1.4

-

Tx-Abf, 60°C

696279

3.2.1.55

1.43

-

native enzyme, pH 5.0, 50°C

732843

3.2.1.55

1.5

2

mutant H98A, pH 5.8, 60°C

731785

3.2.1.55

1.58

-

pH 4.6, 37°C

738310

3.2.1.55

1.6

-

-

288816

3.2.1.55

1.64

-

-

288830

3.2.1.55

1.7

-

mutant enzyme N159A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

1.7

-

pH 7.0, 37°C

656328

3.2.1.55

1.9

-

ph 5.5, 37°C, recombinant wild-type enzyme

732171

3.2.1.55

2.2

-

alpha-L-arafase II

288827

3.2.1.55

2.23

-

in 50 mM phosphate/citrate buffer pH 7.0, at 40°C

715805

3.2.1.55

2.7

-

-

288830

3.2.1.55

3

-

pH 4.1, 25°C, mutant enzyme E310G

678050

3.2.1.55

3.2

-

Tx-Abf-C180A mutant

696279

3.2.1.55

3.4

-

mutant H98F/W99F, pH 5.8, 60°C

731785

3.2.1.55

3.5

-

recombinant His6-tagged enzyme, pH 6.0, 60°C

732329

3.2.1.55

3.6

-

-

288811, 288816, 288822

3.2.1.55

3.7

-

-

677783

3.2.1.55

3.9

-

isoform AbfII, at pH 5.0 and 42°C

744069

3.2.1.55

4

-

-

288816, 288822

3.2.1.55

4.1

-

-

288830

3.2.1.55

4.2

-

mutant W99F, pH 5.8, 60°C

731785

3.2.1.55

4.9

-

-

288816, 288822

3.2.1.55

5

-

-

288818

3.2.1.55

5.1

-

pH 5.3, 25°C, mutant enzyme R290G

678454

3.2.1.55

5.82

-

pH 5.3, 25°C, mutant enzyme F508A

678454

3.2.1.55

6.1

-

pH 5.0, 37°C

732166

3.2.1.55

7.5

-

pH 5.0, 37°C

732166

3.2.1.55

7.97

-

pH 5.3, 25°C, mutant enzyme R290A

678454

3.2.1.55

8.98

-

mutant L352M, pH 7.0, 45°C

737311

3.2.1.55

9.07

-

pH 5.3, 25°C, mutant enzyme R290V

678454

3.2.1.55

9.1

-

mutant W99A, pH 5.8, 60°C

731785

3.2.1.55

10

-

Tx-Abf-M94_I103delinsGG mutant

696279

3.2.1.55

11.5

-

mutant enzyme Y192A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

15

-

mutant H98A/W99A, pH 5.8, 60°C

731785

3.2.1.55

17.7

-

pH 5.3, 25°C, mutant enzyme R290Q

678454

3.2.1.55

20

-

in 0.1 M sodium acetate, pH 6 at 40°C for 30 min

714571

3.2.1.55

26.8

-

pH 5.3, 25°C, mutant enzyme F31A

678454

3.2.1.55

34

-

pH 5.8, 60°C, mutant E28Q

657222

3.2.1.55

40.5

-

pH 5.3, 25°C, mutant enzyme R290K

678454

3.2.1.55

40.7

-

mutant enzyme L289A, in 0.2 M Na2HPO4, 0.1 M citric acid, pH 6.0, at 30°C

715550

3.2.1.55

45

-

Tx-Abf-W99A mutant

696279

3.2.1.55

52.1

-

pH 5.3, 25°C, mutant enzyme R290H

678454

3.2.1.55

94.2

-

isoform AbfI, at pH 5.0 and 37°C

744069

3.2.1.37

14 entries

3.2.1.55

143 entries

3.2.1.58

1.5

-

pH 6.0, 40°C

738437

3.2.1.8

2

3

at pH 5.0 and 50°C

750432

3.2.1.8

65.6

-

pH 5.0, 50°C

656559

3.2.1.8

2 entries

3.2.1.99

5.37

-

pH 4.5, 37°C

750239

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.55

20.8

-

in 50 mM phosphate/citrate buffer pH 7.0, at 40°C

715805

References & Links

Literature References (173)

top print hide

Show Reference (173 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

136275

9872754

Sequence analysis, overexpression, and antisense inhibition of a beta-xylosidase gene, xylA, from Aspergillus oryzae KBN616

1999

Kitamoto, N.; Yoshino, S.; Ohmiya, K.; Tsukagoshi, N.

Appl. Environ. Microbiol.

65

20-24

136279

7574661

Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum

1995

Saxena, S.; Fierobe, H.P.; Gaudin, C.; Guerlesquin, F.; Belaich, J.P.

Appl. Environ. Microbiol.

61

3509-3512

136283

1522062

Purification and characterization of a thermostable beta-xylosidase from Thermoanaerobacter ethanolicus

1992

Shao, W.; Wiegel, J.

J. Bacteriol.

174

5848-5853

136295

-

Characteristics of Trichoderma reesei beta-xylosidase and its use in the hydrolysis of solubilized xylans

1988

Poutanen, K.; Puls, J.

Appl. Microbiol. Biotechnol.

28

425-432

171754

8348546

The purification of commercially available endo-alpha-L-arabinanases and alpha-L-arabinosidase for use in the structural analysis of pectic polysaccharides

1993

Lerouge, P.; O'Neill, M.A.; Darvill, A.G.; Albersheim, P.

Carbohydr. Res.

243

373-378

171764

1814275

Induction, purification and characterisation of arabinases produced by Aspergillus niger

1991

Van der Veen, P.; Flipphi, M.J.A.; Voragen, A.G.J.; Visser, J.

Arch. Microbiol.

157

23-28

208305

-

Xylan-degrading enzyme system produced by the fungus Aspergillus awamori: isolation and characterization of a feruloyl esterase and a p-coumaroyl esterase

1994

McCrae, S.I.; Leith, K.M.; Gordon, A.H.; Wood, T.M.

Enzyme Microb. Technol.

16

826-834

288811

-

An alpha-L-arabinofuranosidase produced by wild-type Streptomyces sp. No. 17-1

1981

Kaji, A.; Sato, M.; Tsutsui, Y.

Agric. Biol. Chem.

45

925-931

288812

-

An alpha-L-arabinofuranosidase from Streptomyces purpurascens IFO 3389

1982

Komae, K.; Kaji, A.; Sato, M.

Agric. Biol. Chem.

46

1899-1905

288813

6742828

alpha-L-Arabinofuranosidase from Ruminococcus albus 8: purification and possible role in hydrolysis of alfalfa cell wall

1984

Greve, L.C.; Labavitch, J.M.; Hungate, R.E.

Appl. Environ. Microbiol.

47

1135-1140

288815

-

Pectic substances, pectic enzymes and haze formation in fruit juices

1984

Whitaker, J.R.

Enzyme Microb. Technol.

6

341-349

288816

-

Purification and characterization of an alpha-L-arabinofuranosidase from Clostridium acetobutylicum ATCC 824

1987

Lee, S.F.; Forsberg, C.W.

Can. J. Microbiol.

33

1011-1016

288817

3663195

Purification and mechanistic properties of an extracellular alpha-L-arabinofuranosidase from Monilinia fructigena

1987

Kelly, M.A.; Sinnott, M.L.; Herrchen, M.

Biochem. J.

245

843-849

288818

-

alpha-L-arabinofuranosidase from Aspergillus niger

1988

Tagawa, K.; Kaji, A.

Methods Enzymol.

160

707-712

288819

-

alpha-L-Arabinofuranosidase from Scopolia japonica

1988

Uchida, T.; Tanaka, M.

Methods Enzymol.

160

712-719

288820

-

Purification and properties of an alpha-L-arabinofuranosidase from cotyledons of soybean seedlings

1991

Hatanaka, H.; Imaoka, H.; Tajima, S.; Kasai, T.

Agric. Biol. Chem.

55

2599-2605

288822

16348679

Purification and characterization of an alpha-L-arabinofuranosidase from Butyrivibrio fibrisolvens GS113

1992

Hespell, R.B.; O'Bryan, P.

Appl. Environ. Microbiol.

58

1082-1088

288823

1622210

Purification and characterization of two alpha-L-arabinofuranosidases from Streptomyces diastaticus

1992

Tajana, E.; Fiechter, A.; Zimmermann, W.

Appl. Environ. Microbiol.

58

1447-1450

288824

-

Characterization and delignification activity of a thermostable alpha-L-arabinofuranosidase from Bacillus stearothermophilus

1993

Bezalel, L.; Shoham, Y.; Rosenberg, E.

Appl. Microbiol. Biotechnol.

40

57-62

288826

7763988

Purification and properties of intracellular alpha-L-arabinofuranosidase from Aspergillus niger 5-16

1993

Kaneko, S.; Shimasaki, T.; Kusakabe, I.

Biosci. Biotechnol. Biochem.

57

1161-1165

288827

-

Characterization of spinach leaf alpha-L-arabinofuranosidases and beta-galactosidases and their synergistic action on an endogenous arabinogalactan-protein

1994

Hirano, Y.; Tsumuraya, Y.; Hashimoto, Y.

Physiol. Plant.

92

286-296

288828

-

Purification and characterization of an alpha-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)

1994

Manin, C.; Shareek, F.; Morosoli, R.; Klueppel, D.

Biochem. J.

302

443-449

288829

-

Production, purification and characterization of an alpha-L-arabinofuranosidase from Bacteroides xylanolyticus X5-1

1994

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