S00151
type: Enzyme
rlcp: p974
cath: Jelly Rolls
ec: https://purl.uniprot.org/enzyme/3.2.1.8
csa: 1bvv
uniprot: P09850
uniprot: Q7SIE3
uniprot: P18429
uniprot: P33557
uniprot: P81536
uniprot: P36217
uniprot: P55329
uniprot: P48793
uniprot: P36218
uniprot: O43097
kegg enzyme: endo-1,4-beta-xylanase
kegg substrate: Xylan
kegg substrate: H2O
kegg product: Xylan
pdb: 1bcxA
pdb: 1bvvA
pdb: 1c5hA
pdb: 1c5iA
pdb: 1hv0A
pdb: 1hv1A
pdb: 1xnbA
pdb: 1xncA
pdb: 2bvvA
pdb: 1qh6A
pdb: 1qh6B
pdb: 1qh7A
pdb: 1qh7B
pdb: 1axkA02
pdb: 1axkB02
pdb: 1bk1A
pdb: 1pvxA
pdb: 1enxA
pdb: 1enxB
pdb: 1redA
pdb: 1redB
pdb: 1reeA
pdb: 1reeB
pdb: 1refA
pdb: 1refB
pdb: 1xyoA
pdb: 1xyoB
pdb: 1xypA
pdb: 1xypB
pdb: 1t6gC
pdb: 1t6gD
pdb: 1ukrA
pdb: 1ukrB
pdb: 1ukrC
pdb: 1ukrD
pdb: 1xndA
pdb: 1xynA
pdb: 1ynaA
active site residues resources: P55329
active site residues resources: P36218
active site residues resources: P36217
active site residues resources: P33557
active site residues resources: P09850
active site residues resources: O43097
active site residues resources: P48793
active site residues resources: P18429
references: Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
references: High-resolution structures of xylanases from B.circulans and T.harzianum identify a new folding pattern and implications for the atomic basis of the catalysis.
references: Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site.
references: Stereochemistry of the hydrolysis of glycosidic linkage by endo-beta-1,4-xylanases of Trichoderma reesei.
references: Crystallization and preliminary X-ray crystallographic studies of thermostable xylanase crystals isolated from Paecilomyces varioti.
references: Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds.
references: Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.
references: Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei.
references: Characterisation of 4-deoxy-beta-L-threo-hex-4-enopyranosyluronic acid attached to xylan in pine kraft pulp and pulping liquor by 1H and 13C NMR spectroscopy.
references: Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei.
references: Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity.
references: The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of bacillus circulans xylanase.
references: Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum.
references: Xylanase homology modeling using the inverse protein folding approach.
references: Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.

Jelly Rolls
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.60.120.180
catalytic domain: index.html

Xylan
type: KeggSubstrate
references: KEGG:C00707
compound type: polysaccharide
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1bcxA
type: Pdb
references: 1bcx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bcx
catalytic residue: TYR 69;GLU 78;TYR 80;
comment: mutant E172C

1bvvA
type: Pdb
references: 1bvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bvv
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172

1c5hA
type: Pdb
references: 1c5h
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c5h
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172
comment: mutant N35D

1c5iA
type: Pdb
references: 1c5i
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c5i
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172
comment: mutant N35D

1hv0A
type: Pdb
references: 1hv0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv0
catalytic residue: TYR 69;GLU 78; ;GLU 172
comment: mutant Y80F

1hv1A
type: Pdb
references: 1hv1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv1
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172
comment: mutant Q127A

1xnbA
type: Pdb
references: 1xnb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xnb
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172

1xncA
type: Pdb
references: 1xnc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xnc
catalytic residue: TYR 69;GLU 78;TYR 80;GLU 172
comment: mutant S100C, N148C

2bvvA
type: Pdb
references: 2bvv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bvv
catalytic residue: ;GLU 78;TYR 80;GLU 172
comment: mutant Y69F

1qh6A
type: Pdb
references: 1qh6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh6
catalytic residue: TYR 85;GLU 94;TYR 96;GLU 184

1qh6B
type: Pdb
references: 1qh6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh6
catalytic residue: TYR 85;GLU 94;TYR 96;GLU 184

1qh7A
type: Pdb
references: 1qh7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh7
catalytic residue: TYR 85;GLU 94;TYR 96;GLU 184

1qh7B
type: Pdb
references: 1qh7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh7
catalytic residue: TYR 85;GLU 94;TYR 96;GLU 184

1axkA02
type: Pdb
references: 1axk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1axk
catalytic residue: TYR 225;GLU 234;TYR 236;GLU 328

1axkB02
type: Pdb
references: 1axk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1axk
catalytic residue: TYR 225;GLU 234;TYR 236;GLU 328

1bk1A
type: Pdb
references: 1bk1
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bk1
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1pvxA
type: Pdb
references: 1pvx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pvx
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 178

1enxA
type: Pdb
references: 1enx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1enx
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1enxB
type: Pdb
references: 1enx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1enx
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1redA
type: Pdb
references: 1red
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1red
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1redB
type: Pdb
references: 1red
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1red
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1reeA
type: Pdb
references: 1ree
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ree
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1reeB
type: Pdb
references: 1ree
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ree
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1refA
type: Pdb
references: 1ref
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ref
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1refB
type: Pdb
references: 1ref
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ref
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1xyoA
type: Pdb
references: 1xyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xyo
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1xyoB
type: Pdb
references: 1xyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xyo
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1xypA
type: Pdb
references: 1xyp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xyp
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1xypB
type: Pdb
references: 1xyp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xyp
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1t6gC
type: Pdb
references: 1t6g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t6g
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1t6gD
type: Pdb
references: 1t6g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t6g
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1ukrA
type: Pdb
references: 1ukr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukr
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1ukrB
type: Pdb
references: 1ukr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukr
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1ukrC
type: Pdb
references: 1ukr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukr
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1ukrD
type: Pdb
references: 1ukr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ukr
catalytic residue: TYR 70;GLU 79;TYR 81;GLU 170

1xndA
type: Pdb
references: 1xnd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xnd
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 177

1xynA
type: Pdb
references: 1xyn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xyn
catalytic residue: TYR 66;GLU 75;TYR 77;GLU 164

1ynaA
type: Pdb
references: 1yna
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yna
catalytic residue: TYR 77;GLU 86;TYR 88;GLU 178

Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1886523
journal: Microbiol Rev
volume: 55
pages: 303-15
published year: 1991
authors:
  item: Gilkes NR
  item: Henrissat B
  item: Kilburn DG
  item: Miller RC Jr
  item: Warren RA

High-resolution structures of xylanases from B.circulans and T.harzianum identify a new folding pattern and implications for the atomic basis of the catalysis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) (ISBN: 9518913625)
journal: TRICEL Symposium on Trichoderma Reesei Cellulases and Other Hydrolases
pages: 63-72
published year: 1993
authors:
  item: Campbell RL
  item: Rose DR
  item: Wakarchuk WW
  item: To RJ
  item: Sung W
  item: Yaguchi M
references: P48793

Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
medline id: 94283373
references: http://www.ncbi.nlm.nih.gov/pubmed/8013449
journal: EMBO J
volume: 13
pages: 2493-501
published year: 1994
authors:
  item: Torronen A
  item: Harkki A
  item: Rouvinen J
references: P36217

Stereochemistry of the hydrolysis of glycosidic linkage by endo-beta-1,4-xylanases of Trichoderma reesei.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7988708
journal: FEBS Lett
volume: 356
pages: 137-40
published year: 1994
authors:
  item: Biely P
  item: Kremnicky L
  item: Alfoldi J
  item: Tenkanen M

Crystallization and preliminary X-ray crystallographic studies of thermostable xylanase crystals isolated from Paecilomyces varioti.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7966300
journal: J Mol Biol
volume: 243
pages: 806-8
published year: 1994
authors:
  item: Eswaramoorthy S
  item: Vithayathil PJ
  item: Viswamitra MA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7700870
journal: Protein Eng
volume: 7
pages: 1379-86
published year: 1994
authors:
  item: Wakarchuk WW
  item: Sung WL
  item: Campbell RL
  item: Cunningham A
  item: Watson DC
  item: Yaguchi M

Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS.
medline id: 94290322
references: http://www.ncbi.nlm.nih.gov/pubmed/8019418
journal: Protein Sci
volume: 3
pages: 467-75
published year: 1994
authors:
  item: Wakarchuk WW
  item: Campbell RL
  item: Sung WL
  item: Davoodi J
  item: Yaguchi M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P09850

Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 95127663
references: http://www.ncbi.nlm.nih.gov/pubmed/7827044
journal: Biochemistry
volume: 34
pages: 847-56
published year: 1995
authors:
  item: Torronen A
  item: Rouvinen J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P36218
references: P36217

Characterisation of 4-deoxy-beta-L-threo-hex-4-enopyranosyluronic acid attached to xylan in pine kraft pulp and pulping liquor by 1H and 13C NMR spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7648585
journal: Carbohydr Res
volume: 272
pages: 55-71
published year: 1995
authors:
  item: Teleman A
  item: Harjunpaa V
  item: Tenkanen M
  item: Buchert J
  item: Hausalo T
  item: Drakenberg T
  item: Vuorinen T

Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
medline id: 96302263
references: http://www.ncbi.nlm.nih.gov/pubmed/8755744
journal: Biochemistry
volume: 35
pages: 9617-24
published year: 1996
authors:
  item: Havukainen R
  item: Torronen A
  item: Laitinen T
  item: Rouvinen J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P36217

Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8756474
journal: Biochemistry
volume: 35
pages: 10110-8
published year: 1996
authors:
  item: Lawson SL
  item: Wakarchuk WW
  item: Withers SG

The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of bacillus circulans xylanase.
type: BibliographicResource
comment: STRUCTURE BY NMR.
medline id: 96322313
references: http://www.ncbi.nlm.nih.gov/pubmed/8756457
journal: Biochemistry
volume: 35
pages: 9958-66
published year: 1996
authors:
  item: McIntosh LP
  item: Hand G
  item: Johnson PE
  item: Joshi MD
  item: Korner M
  item: Plesniak LA
  item: Ziser L
  item: Wakarchuk WW
  item: Withers SG
references: P09850

Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
medline id: 97045991
references: http://www.ncbi.nlm.nih.gov/pubmed/8890913
journal: J Mol Biol
volume: 263
pages: 70-8
published year: 1996
authors:
  item: Krengel U
  item: Dijkstra BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P55329

Xylanase homology modeling using the inverse protein folding approach.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8845760
journal: Protein Sci
volume: 5
pages: 705-8
published year: 1996
authors:
  item: Chen X
  item: Whitmire D
  item: Bowen JP

Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8931150
journal: Protein Sci
volume: 5
pages: 2319-28
published year: 1996
authors:
  item: Plesniak LA
  item: Connelly GP
  item: Wakarchuk WW
  item: McIntosh LP

Secondary structure and NMR assignments of Bacillus circulans xylanase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8762143
journal: Protein Sci
volume: 5
pages: 1118-35
published year: 1996
authors:
  item: Plesniak LA
  item: Wakarchuk WW
  item: McIntosh LP

Endo-beta-1,4-xylanase families: differences in catalytic properties.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9335171
journal: J Biotechnol
volume: 57
pages: 151-66
published year: 1997
authors:
  item: Biely P
  item: Vrsanska M
  item: Tenkanen M
  item: Kluepfel D

Structural and functional properties of low molecular weight endo-1,4-beta-xylanases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9335170
journal: J Biotechnol
volume: 57
pages: 137-49
published year: 1997
authors:
  item: Torronen A
  item: Rouvinen J

Complete measurement of the pKa values of the carboxyl and imidazole groups in Bacillus circulans xylanase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9416621
journal: Protein Sci
volume: 6
pages: 2667-70
published year: 1997
authors:
  item: Joshi MD
  item: Hedberg A
  item: McIntosh LP

Catalytic thiol and carboxylate: role of cysteine and glutamic acid in the xylosidic activity of endoxylanase from Chainia sp. (NCL 82-5-1).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9675021
journal: Arch Biochem Biophys
volume: 355
pages: 153-9
published year: 1998
authors:
  item: Subray SH
  item: Ameeta RK
  item: Krishna NG
  item: Khan IM

Mechanisms of cellulases and xylanases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9649739
journal: Biochem Soc Trans
volume: 26
pages: 156-60
published year: 1998
authors:
  item: Birsan C
  item: Johnson P
  item: Joshi M
  item: MacLeod A
  item: McIntosh L
  item: Monem V
  item: Nitz M
  item: Rose DR
  item: Tull D
  item: Wakarchuck WW
  item: Wang Q
  item: Warren RA
  item: White A
  item: Withers SG

Characterization of a buried neutral histidine in Bacillus circulans xylanase: internal dynamics and interaction with a bound water molecule.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9485306
journal: Biochemistry
volume: 37
pages: 1810-8
published year: 1998
authors:
  item: Connelly GP
  item: McIntosh LP

Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
medline id: 98426042
references: http://www.ncbi.nlm.nih.gov/pubmed/9753433
journal: Biochemistry
volume: 37
pages: 13475-85
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Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH.
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Purification and biochemical characteristics of beta-D-xylanase from a thermophilic fungus, Thermomyces lanuginosus-SSBP.
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Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.
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Structure of XynB, a highly thermostable beta-1,4-xylanase from Dictyoglomus thermophilum Rt46B.1, at 1.8 A resolution.
type: BibliographicResource
comment: X-ray crystallography
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Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei.
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Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase.
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comment: X-ray crystallography
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The tertiary structure at 1.59 A resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier.
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Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate.
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Oligosaccharide binding to family 11 xylanases: both covalent intermediate and mutant product complexes display (2,5)B conformations at the active centre.
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Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase.
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A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermal stability through synergism.
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Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger.
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Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH.
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Mapping the conformational itinerary of beta-glycosidases by X-ray crystallography.
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MM-PBSA free energy analysis of endo-1,4-xylanase II (XynII)-substrate complexes: binding of the reactive sugar in a skew boat and chair conformation.
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Long-range nature of the interactions between titratable groups in Bacillus agaradhaerens family 11 xylanase: pH titration of B. agaradhaerens xylanase.
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Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I.
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endo-(1->4)-beta-xylan 4-xylanohydrolase
type: KeggEnzyme

endo-1,4-xylanase
type: KeggEnzyme

xylanase
type: KeggEnzyme

beta-1,4-xylanase
type: KeggEnzyme

endo-1,4-xylanase
type: KeggEnzyme

endo-beta-1,4-xylanase
type: KeggEnzyme

endo-1,4-beta-D-xylanase
type: KeggEnzyme

1,4-beta-xylan xylanohydrolase
type: KeggEnzyme

beta-xylanase
type: KeggEnzyme

beta-1,4-xylan xylanohydrolase
type: KeggEnzyme

endo-1,4-beta-xylanase
type: KeggEnzyme

beta-D-xylanase
type: KeggEnzyme

Analogue
compound: Xylan
pdb: 1qh7A
ligand het code: XYP

Analogue
compound: Xylan
pdb: 1qh7B
ligand het code: XYP

IntermediateAnalogue
pdb: 1bvvA
ligand het code: XYP-DFX

IntermediateAnalogue
pdb: 1c5iA
ligand het code: XYP-DFX

IntermediateAnalogue
pdb: 1qh6A
ligand het code: FXP

IntermediateAnalogue
pdb: 1qh6B
ligand het code: FXP

IntermediateAnalogue
pdb: 1redB
ligand het code: C5X

IntermediateAnalogue
pdb: 1reeB
ligand het code: C4X

IntermediateAnalogue
pdb: 1refB
ligand het code: C3X

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.68

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.2499-2500

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1, p.471-473

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.851-853

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.9624

ReferenceForCatalyticMechanism
reference index: 11
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.1, Fig.3, p.9964-9965

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.74-76

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.4, p.143-145

ReferenceForCatalyticMechanism
reference index: 21
reference section: Fig.1, Fig.2

ReferenceForCatalyticMechanism
reference index: 23

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig.1, Fig.6

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.486-487

ReferenceForCatalyticMechanism
reference index: 32
reference section: Fig.10, p.268-271

ReferenceForCatalyticMechanism
reference index: 37
reference section: Fig.1, p.1012410-10128

ReferenceForCatalyticMechanism
reference index: 43
reference section: Scheme 1, Scheme 3, p.525

ReferenceForCatalyticMechanism
reference index: 44
reference section: Fig. 1, p.3539