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• • Molecular Structure
  • Sum Formula
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  • InChIKey
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• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
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Ligand birchwood xylan

Basic Ligand Information

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.73

birchwood xylan + H2O = ferulic acid + ?

208317

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-alpha-D-glucuronic acid + ?

732277

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-alpha-D-glucuronic acid + glucuronic acid

732167

-

3.2.1.131

2 entries

3.2.1.55

birchwood xylan + H2O = L-arabinose + ?

288830, 288841, 714571

-

Substrate in Enzyme-catalyzed Reactions (41 results)

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Show Substrate (41 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.6

birchwood xylan + H2O = ?

730602

-

3.1.1.72

birchwood xylan + H2O = ?

713864

-

3.1.1.73

birchwood xylan + H2O = ferulic acid + ?

208317

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-alpha-D-glucuronic acid + ?

732277, 746695

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-alpha-D-glucuronic acid + D-glucuronic acid

713669

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-alpha-D-glucuronic acid + glucuronic acid

732167

-

3.2.1.131

birchwood xylan + H2O = 4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?

738687

-

3.2.1.131

4 entries

3.2.1.136

birchwood xylan + H2O = ?

737360

-

3.2.1.139

birchwood xylan + H2O = 4-O-methyl-D-glucuronic acid + D-glucuronic acid

713669

-

3.2.1.139

birchwood xylan + H2O = 4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?

738687

-

3.2.1.139

birchwood xylan + H2O = 4-O-methylglucuronic acid + ?

745060

-

3.2.1.139

birchwood xylan + H2O = 4-O-methylglucuronoxylan + ?

737908

-

3.2.1.139

birchwood xylan + H2O = ?

732877, 732167, 732277

-

3.2.1.37

birchwood xylan + H2O = ?

746353

-

3.2.1.37

birchwood xylan + H2O = beta-D-xylose + ?

750780

-

3.2.1.37

birchwood xylan + H2O = D-xylose

737855

-

3.2.1.139

5 entries

3.2.1.37

3 entries

3.2.1.4

birchwood xylan + H2O = ?

729084, 735783, 692258, 736374, 746553, 750783

-

3.2.1.55

birchwood xylan + H2O = ?

732745

-

3.2.1.55

birchwood xylan + H2O = L-arabinose + ?

288830, 288841, 714571

-

3.2.1.55

2 entries

3.2.1.6

birchwood xylan + H2O = ?

729084

-

3.2.1.8

birchwood xylan + H2O = ?

680969, 679573, 680984, 752334, 746374, 746350, 677745, 742216, 741504, 742165, 742400, 695689, 741629, 742661, 738886, 738196, 742470, 654986, 677613, 677960, 696858, 699042, 699489, 680958, 742765, 730191, 730370, 730881, 731026, 745416, 742106, 742680, 745147, 744124, 748630, 749504, 677623, 730187, 751347, 679547, 679721, 699498, 697502, 695668, 752084, 692258, 731024, 743097, 742214, 750679, 750084, 750783, 750448

-

3.2.1.8

birchwood xylan + H2O = D-xylose

678008

-

3.2.1.8

birchwood xylan + H2O = D-xylose + ?

696797, 731022

-

3.2.1.8

birchwood xylan + H2O = D-xylose + L-arabinose + xylobiose + ?

697503

-

3.2.1.8

birchwood xylan + H2O = D-xylose + xylobiose + ?

695838, 695801

-

3.2.1.8

birchwood xylan + H2O = D-xylose + xylobiose + xylotriose

695696

-

3.2.1.8

birchwood xylan + H2O = D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose

695678

-

3.2.1.8

birchwood xylan + H2O = xylo-oligosaccharides

737510, 682991

-

3.2.1.8

birchwood xylan + H2O = xylo-oligosaccharides + ?

737935, 737851, 738547, 737466, 737727, 737855, 738192

-

3.2.1.8

birchwood xylan + H2O = xylobiose

750497, 749635

-

3.2.1.8

birchwood xylan + H2O = xylobiose + ?

742131

-

3.2.1.8

birchwood xylan + H2O = xylobiose + xylose + ?

737477

-

3.2.1.8

birchwood xylan + H2O = xylobiose + xylotetraose + ?

699053

-

3.2.1.8

birchwood xylan + H2O = xylobiose + xylotriose

752115, 750497, 746962

-

3.2.1.8

birchwood xylan + H2O = xylohexaose

738862

-

3.2.1.8

birchwood xylan + H2O = xylooligosaccharides

717094

-

3.2.1.8

birchwood xylan + H2O = xylose

696797

-

3.2.1.8

birchwood xylan + H2O = xylose + ?

681711, 699358

-

3.2.1.8

birchwood xylan + H2O = xylose + xylo-oligosaccharides

737475

-

3.2.1.8

birchwood xylan + H2O = xylose + xylobiose

738862

-

3.2.1.8

birchwood xylan + H2O = xylotetraose + xylotriose + xylobiose + xylose

745089

-

3.2.1.8

21 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.72

acetylated birchwood xylan + H2O = acetate + birchwood xylan

-

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.176

mixed inhibition

736090

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (52 results)

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Show Turnover Number (52 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.2.1.131

0.008

-

mutant R331A, pH 6.5, 40°C

738687

3.2.1.131

0.3

-

mutant E381A, pH 6.5, 40°C

738687

3.2.1.131

1

-

mutant D215A, pH 6.5, 40°C

738687

3.2.1.131

11.1

-

in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37°C

732167

3.2.1.131

86

-

mutant F696A, pH 6.5, 40°C

738687

3.2.1.131

116

-

mutant W689A, pH 6.5, 40°C

738687

3.2.1.131

129

-

mutant W773A, pH 6.5, 40°C

738687

3.2.1.131

289

-

wild-type, pH 6.5, 40°C

738687

3.2.1.139

0.008

-

mutant R331A, pH 6.5, 40°C

738687

3.2.1.139

0.3

-

mutant E381A, pH 6.5, 40°C

738687

3.2.1.139

1

-

mutant D215A, pH 6.5, 40°C

738687

3.2.1.139

11.08

-

recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate

732167

3.2.1.139

14.37

-

recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate

732167

3.2.1.139

19.4

-

at pH 4.0 and 50°C

745060

3.2.1.139

86

-

mutant F696A, pH 6.5, 40°C

738687

3.2.1.139

116

-

mutant W689A, pH 6.5, 40°C

738687

3.2.1.139

129

-

mutant W773A, pH 6.5, 40°C

738687

3.2.1.139

289

-

wild-type, pH 6.5, 40°C

738687

3.2.1.55

0.45

-

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

732745

3.2.1.55

0.48

-

pH 5.7, 50°C, recombinant catalytic module CtGH43

732745

3.2.1.8

0.039

-

wild type enzyme, at pH 7.0

680984

3.2.1.8

0.039

-

wild-type

680984

3.2.1.8

1.7

-

pH 7.5, 50°C

752334

3.2.1.8

2

-

in 48.5 mM citric acid and 103 mM disodium hydrogen phosphate, pH 5, at 40°C

677960

3.2.1.8

2

-

mutant W9Y/N35D

680984

3.2.1.8

4.26

-

pH 6.5, 50°C

742680

3.2.1.8

8.8

-

mutant R112Y

680984

3.2.1.8

10.5

-

isozyme IIc, pH 6.0, 70°C

654986

3.2.1.8

14.6

-

mutant Q127K

680984

3.2.1.8

21

-

mutant Y174W

680984

3.2.1.8

36.8

-

His-tagged enzyme, pH 6.0, 40°C

752084

3.2.1.8

39

-

mutant D11F/R122D

680984

3.2.1.8

50.7

-

mutant N35D

680984

3.2.1.8

65.4

-

mutant G12W

680984

3.2.1.8

71.6

-

mutant W9Y/N35D

680984

3.2.1.8

72.07

-

in 48.5 mM citric acid and 103 mM disodium hydrogen phosphate, pH 5, at 40°C

677960

3.2.1.8

73

-

isozyme IIa, pH 6.0, 70°C

654986

3.2.1.8

88.7

-

mutant W9Y

680984

3.2.1.8

103.4

-

-

699489

3.2.1.8

111.2

-

mutant Y174W

680984

3.2.1.8

125.9

-

pH 6.0, 50°C

737477

3.2.1.8

140.1

-

wild type enzyme, at pH 7.0

680984

3.2.1.8

140.1

-

wild-type

680984

3.2.1.8

222

-

pH 6.0, 65°C

745089

3.2.1.8

245

-

recombinant enzyme, pH 5.0, 55°C

752115

3.2.1.8

277

-

apparent value for the native enzyme

677745

3.2.1.8

292

-

apparent value for the recombinant enzyme

677745

3.2.1.8

465

-

pH 5.5, 85°C

742470

3.2.1.8

872

-

apparent value for the native enzyme

677745

3.2.1.8

997

-

apparent value for the recombinant enzyme

677745

3.2.1.8

1737

-

-

695696

3.2.1.8

7764

-

Km value is 2.95 mg/ml, pH 5.0, 50°C

731024

3.2.1.131

8 entries

3.2.1.139

10 entries

3.2.1.55

2 entries

3.2.1.8

32 entries

K_M Value (26 results)

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Show KM Value (26 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.1.72

16.72

-

pH 8.2, 58°C

713864

3.2.1.131

-999

-

km value of wild-type 43 mg/ml, pH 6.5, 40°C

738687

3.2.1.131

0.3

-

in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37°C

732167

3.2.1.139

-999

-

km vaule of wild-type 43 mg/ml, pH 6.5, 40°C

738687

3.2.1.139

0.3

-

recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate

732167

3.2.1.139

1.1

-

recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate

732167

3.2.1.131

2 entries

3.2.1.139

3 entries

3.2.1.4

-999

-

Km value 4.37 mg/ml, pH 5.0, temperature not specified in the publication

746553

3.2.1.55

0.9

-

pH 5.7, 50°C, recombinant catalytic module CtGH43

732745

3.2.1.55

0.95

-

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

732745

3.2.1.8

-999

-

Km value 0.55 mg/ml, pH 5.5, 85°C

738196, 742470

3.2.1.8

-999

-

Km value 0.9 mg/ml, pH 7, 65°C

738547

3.2.1.8

-999

-

Km value 1.05 mg/ml, pH 6.5, 65°C

738862

3.2.1.8

-999

-

Km value 1.44 mg/ml, pH 5.0, 50°C

745416

3.2.1.8

-999

-

Km value 1.5 mg/ml, pH 6.0, 65°C

745089

3.2.1.8

-999

-

Km value 10.5 mg/ml, pH 6.5, 80°C

738862

3.2.1.8

-999

-

Km value 11.7 mg/ml, pH 5.0, 50°C

737935

3.2.1.8

-999

-

Km value 22.5 mg/ml, pH 7.0, 50°C

741629

3.2.1.8

-999

-

Km value 3.0 mg/ml, pH 6.5, 65°C

738862

3.2.1.8

-999

-

Km value 3.26 mg/ml, pH 6.5, 50°C

742131

3.2.1.8

-999

-

Km value 4.39 mg/ml, pH 6.0, 50°C

737477

3.2.1.8

-999

-

Km value 7.1 mg/ml, pH 6.5, 50°C

742680

3.2.1.8

-999

-

Km value is 2.95 mg/ml, pH 5.0, 50°C

731024

3.2.1.8

-999

-

Km value is 28.3 mg/ml, pH 6.5, 65°C

730187

3.2.1.8

-999

-

Km value is 4.4 mg/ml, pH 11, 70°C

731022

3.2.1.8

-999

-

pH 6.0, 95°C, Km-value: 3.5 mg/ml

748630

3.2.1.8

-999

-

truncated variant XynAGN16L, Km value 2.6 mg/ml, truncated variant 1.2 mg/ml, respcetively, pH 6.5, 37°C

737475

3.2.1.55

2 entries

3.2.1.8

17 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.176

-999

-

Kic 0.093 g/l, Kiu 0.18 g/l, pH 5.0, 37°C

736090

References & Links

Literature References (106)

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Show Reference (106 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

208317

10747226

Purification and characterization of an extracellular feruloyl esterase from the thermophilic anaerobe Clostridium stercorarium

2000

Donaghy, J.A.; Bronnenmeier, K.; Soto-Kelly, P.F.; McKay, A.M.

J. Appl. Microbiol.

88

458-466

288830

8125239

alpha-L-arabinofuranosidase production by Aspergillus nidulans

1994

Fernandez-Espinar, M.T.; Pena, J.L.; Pinaga, F.; Valles, S.

FEMS Microbiol. Lett.

115

107-112

288841

10656340

An alpha-L-arabinofuranosidase from Penicillium purpurogenum: Production, purification and properties

2000

De Ioannes, P.; Peirano, A.; Steiner, J.; Eyzaguirre, J.

J. Biotechnol.

76

253-258

654986

10923787

Purification, characterization and substrate specificities of xylanase isoenzymes from Melanocarpus albomyces IIS 68

2000

Saraswat, V.; Bisaria, V.S.

Biosci. Biotechnol. Biochem.

64

1173-1180

677613

18027102

Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12

2007

Oh, H.W.; Heo, S.Y.; Kim, D.Y.; Park, D.S.; Bae, K.S.; Park, H.Y.

Antonie van Leeuwenhoek

93

437-442

677623

16915648

Purification and characterization of two xylanases from alkalophilic and thermophilic Bacillus licheniformis 77-2

2006

Damiano, V.B.; Ward, R.; Gomes, E.; Alves-Prado, H.F.; Da Silva, R.

Appl. Biochem. Biotechnol.

129-132

289-302

677745

17216454

Substrate and product hydrolysis specificity in family 11 glycoside hydrolases: an analysis of Penicillium funiculosum and Penicillium griseofulvum xylanases

2007

Berrin, J.G.; Ajandouz, e.l.H.; Georis, J.; Arnaut, F.; Juge, N.

Appl. Microbiol. Biotechnol.

74

1001-1010

677960

17383610

Unprocessed barley aleurone endo-beta-1,4-xylanase X-I is an active enzyme

2007

Van Campenhout, S.; Pollet, A.; Bourgois, T.M.; Rombouts, S.; Beaugrand, J.; Gebruers, K.; De Backer, E.; Courtin, C.M.; Delcour, J.A.; Volckaert, G.

Biochem. Biophys. Res. Commun.

356

799-804

678008

-

Purification and properties of a xylanase produced by Bacillus circulans BL53 on solid-state cultivation

2006

Heck, J.X.; Soares, L.H.; Hertz, P.F.; Ayub, M.A.

Biochem. Eng. J.

32

179-184

679547

-

A thermostable alkaline active endo-beta-1-4-xylanase from Bacillus halodurans S7: Purification and characterization

2006

Mamo, G.; Hatti-Kaul, R.; Mattiasson, B.

Enzyme Microb. Technol.

39

1492-1498

679573

-

Cloning, expression, characterization, and high cell-density production of recombinant endo-1,4-beta-xylanase from Aspergillus niger in Pichia pastoris

2007

Ruanglek, V.; Sriprang, R.; Ratanaphan, N.; Tirawongsaroj, P.; Chantasigh, D.; Tanapongpipat, S.; Pootanakit, K.; Eurwilaichitr, L.

Enzyme Microb. Technol.

41

19-25

679721

15064978

A xylan-degrading strain of Sulfolobus solfataricus: isolation and characterization of the xylanase activity

2004

Cannio, R.; Di Prizito, N.; Rossi, M.; Morana, A.

Extremophiles

8

117-124

680958

16139382

Increased alkali stability in Trichoderma reesei endo-1,4-beta-xylanase II by site directed mutagenesis

2006

Fenel, F.; Zitting, A.; Kantelinen, A.

J. Biotechnol.

121

102-107

680969

16919348

Engineering a de novo internal disulfide bridge to improve the thermal stability of xylanase from Bacillus stearothermophilus No. 236

2007

Jeong, M.Y.; Kim, S.; Yun, C.W.; Choi, Y.J.; Cho, S.G.

J. Biotechnol.

127

300-309

680984

17445930

Targeted molecular engineering of a family 11 endoxylanase to decrease its sensitivity towards Triticum aestivum endoxylanase inhibitor types

2007

Bourgois, T.M.; Nguyen, D.V.; Sansen, S.; Rombouts, S.; Belien, T.; Fierens, K.; Raedschelders, G.; Rabijns, A.; Courtin, C.M.; Delcour, J.A.; Van Campenhout, S.; Volckaert, G.

J. Biotechnol.

130

95-105

681711

17257262

A novel cellulase free alkaliphilic xylanase from alkali tolerant Penicillium citrinum: production, purification and characterization

2007

Dutta, T.; Sengupta, R.; Sahoo, R.; Sinha Ray, S.; Bhattacharjee, A.; Ghosh, S.

Lett. Appl. Microbiol.

44

206-211

682991

100112087

Purification and characterization of a high molecular weight endoxylanase from the solid-state culture of an alkali-tolerant Aspergillus fumigatus MKU1

2006

Thiagarajan, S.; Jeya, M.; Gunasekaran, P.

World J. Microbiol. Biotechnol.

22

487-492

692258

18568289

Evidence that the xylanase activity from Sulfolobus solfataricus Oalpha is encoded by the endoglucanase precursor gene (sso1354) and characterization of the associated cellulase activity

2008

Maurelli, L.; Giovane, A.; Esposito, A.; Moracci, M.; Fiume, I.; Rossi, M.; Morana, A.

Extremophiles

12

689-700

695668

18607546

Production and characterization of cellulase-free xylanase from Trichoderma inhamatum

2008

De Oliveira da Silva, L.A.; Carmona, E.C.

Appl. Biochem. Biotechnol.

150

117-125

695678

18688581

Hydrolytic properties of a hybrid xylanase and its parents

2009

Sun, J.Y.; Liu, M.Q.; Weng, X.Y.

Appl. Biochem. Biotechnol.

152

428-439

695689

18668373

Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization

2009

Maalej, I.; Belhaj, I.; Masmoudi, N.F.; Belghith, H.

Appl. Biochem. Biotechnol.

158

200-212

695696

19002659

Cloning, expression, and characterization of a new Streptomyces sp. S27 xylanase for which xylobiose is the main hydrolysis product

2008

Li, N.; Shi, P.; Yang, P.; Wang, Y.; Luo, H.; Bai, Y.; Zhou, Z.; Yao, B.

Appl. Biochem. Biotechnol.

159

521-531

695801

18521591

Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces sp. S9

2008

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A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans

2016

Verma, A.; Goyal, A.

J. Mol. Catal. B

129

6-14

752084

-

Molecular characterization of a first endo-acting beta-1,4-xylanase of family 10 glycoside hydrolase (PsGH10A) from Pseudopedobacter saltans comb. nov

2018

Sharma, K.; Antunes, I.; Rajulapati, V.; Goyal, A.

Process Biochem.

70

79-89

752115

30923012

Efficient expression and secretion of endo-1,4-beta-xylanase from Penicillium citrinum in non-conventional yeast Yarrowia lipolytica directed by the native and the preproLIP2 signal peptides

2019

Ouephanit, C.; Boonvitthya, N.; Theerachat, M.; Bozonnet, S.; Chulalaksananukul, W.

Protein Expr. Purif.

160

1-6

752334

30706219

Delineating thermophilic xylanase from Bacillus licheniformis DM5 towards its potential application in xylooligosaccharides production

2019

Ghosh, A.; Sutradhar, S.; Baishya, D.

World J. Microbiol. Biotechnol.

35

34

Links to other databases for birchwood xylan

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PubChem

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Release 2021.2 (July 2021)
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